enzyme_display_name: Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

column_label: Supplemental Table S1 PhnM section row RPnTP column Km (uM)=56 +/- 12

raw_value_unit_evidence: Supplemental Table S1 row RPnTP: Km=56 +/- 12 uM

row_label: RPnTP

table_label: Supplemental Table S1: Kinetic constants for the reactions catalyzed by PhnI and PhnM


organism: Escherichia coli (strain K12)

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Supplemental Table S1 PhnM section row RTP column Km (uM)=98 +/- 12

raw_value_unit_evidence: Supplemental Table S1 row RTP: Km=98 +/- 12 uM

row_label: RTP

data_origin: experimental

enzyme: Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

status: verified

source: uniprot


column_label: Supplemental Table S1 PhnM section row RDP column Km (uM)=200 +/- 32

raw_value_unit_evidence: Supplemental Table S1 row RDP: Km=200 +/- 32 uM

row_label: RDP


enzyme_display_name: UniProt Q9WPH5

organism: Hepacivirus C

substrate_name: ATP

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt Q9WPH5

substrate: ATP

source: skid


enzyme_display_name: UniProt P38919

organism: Homo sapiens

enzyme: UniProt P38919


enzyme_display_name: UniProt Q9Q6P4

organism: West Nile virus

enzyme: UniProt Q9Q6P4


enzyme_display_name: Genome polyprotein

organism: Hepatitis GB virus B

substrate_name: ATP for NS3 NTPase

verification_status: unverified

enzyme: Genome polyprotein

substrate: ATP for NS3 NTPase

status: unverified


substrate_name: CTP for NS3 NTPase

substrate: CTP for NS3 NTPase


substrate_name: UTP for NS3 NTPase

substrate: UTP for NS3 NTPase


substrate_name: dATP for NS3 NTPase

substrate: dATP for NS3 NTPase


substrate_name: dCTP for NS3 NTPase

substrate: dCTP for NS3 NTPase


substrate_name: dTTP for NS3 NTPase

substrate: dTTP for NS3 NTPase


enzyme_display_name: UniProt Q980M3

organism: Saccharolobus solfataricus

substrate_name: GTP

proof_lines:
Raw SKiD Env: Temp=50°C, pH=7.5
Raw SKiD Env: Temp=50°C, pH=7.4
Raw SKiD Env: Temp=50°C, pH=7.8

enzyme: UniProt Q980M3

substrate: GTP


enzyme_display_name: UniProt Q980A5

proof_lines:
Raw SKiD Env: Temp=60°C, pH=-----
Raw SKiD Env: Temp=50°C, pH=7.8
Raw SKiD Env: Temp=75°C, pH=7.8

enzyme: UniProt Q980A5


enzyme_display_name: UniProt P60785

organism: Escherichia coli

enzyme: UniProt P60785


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase DDP1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

assay_conditions_summary: cofactor ADP

column_label: Table I, row Ap6A, column Km (microM)=56; same row products=p4A + ADP (76%); p5A + AMP (24%), kcat=0.4 s^-1.

raw_value_unit_evidence: Ap6A: Km=56 microM; products=p4A + ADP (76%); p5A + AMP (24%); Vmax=1 units mg^-1; kcat=0.4 s^-1; kcat/Km=6.4 x10^3 M^-1 s^-1

table_label: Table I. Products and kinetic constants


enzyme: Diphosphoinositol polyphosphate phosphohydrolase DDP1


assay_conditions_summary: cofactor ATP


enzyme_display_name: GTP cyclohydrolase II

source_db: brenda

enzyme: GTP cyclohydrolase II

source: brenda


enzyme_display_name: alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

source_db: oed

verification_status: corrected

column_label: Supplemental Table S1 PhnM section row RPnTP columns kcat (s^-1)=6.4 +/- 0.3, Km (uM)=56 +/- 12, kcat/Km (M^-1s^-1)=(1.1 +/- 0.2) x 10^5

normalized_value_unit_evidence: kcat 6.4 s^-1 from explicit paper cell; kcat_over_km 110 s^-1 mM^-1 from explicit paper cell; km 0.056 mM from explicit paper cell

status: corrected

source: oed


substrate_name: D-Ribose 5-diphosphate

kcat_over_km_origin: calculated

column_label: Supplemental Table S1 PhnM section row RDP columns kcat (s^-1)=0.08 +/- 0.01, Km (uM)=200 +/- 32, kcat/Km (M^-1s^-1)=(0.38 +/- 0.03) x 10^3

normalized_value_unit_evidence: kcat=0.08 s^-1; Km=0.200 mM; kcat_over_km=0.4 s^-1*mM^-1 from kcat/Km cells; table ratio column rounds to 0.38 s^-1*mM^-1

enzyme: alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase

substrate: D-Ribose 5-diphosphate


substrate_name: D-Ribose 5-phosphate

proof_lines: D-ribose-5-phosphate pyrophosphate RTP

substrate: D-Ribose 5-phosphate


enzyme_display_name: UniProt P83788

organism: Pseudomonas fluorescens

km_display: Not reported

enzyme: UniProt P83788


substrate_name: L-kynurenine

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

substrate: L-kynurenine


substrate_name: O-benzoyl-L-serine

substrate: O-benzoyl-L-serine


enzyme_display_name: UniProt Q8NFP7

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

sequence_source: multiple

source_databases_merged: skid uniprot

enzyme: UniProt Q8NFP7


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 3-alpha

column_label: Table I row PP-InsP5, hDIPP3-alpha, Km column.

normalized_value_unit_evidence: 0.088 uM normalizes to 0.000088 mM.

raw_value_unit_evidence: Table I reports PP-InsP5 alpha Km 0.088 uM.

row_label: PP-InsP5, isoform alpha / hDIPP3-alpha

table_label: Table I, Catalytic properties of the hDIPP3 isoforms


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 3-beta

column_label: Table I row PP-InsP5, hDIPP3-beta, Km column.

normalized_value_unit_evidence: 0.053 uM normalizes to 0.000053 mM.

raw_value_unit_evidence: Table I reports PP-InsP5 beta Km 0.053 uM.

row_label: PP-InsP5, isoform beta / hDIPP3-beta


column_label: Table I row Ap6A, hDIPP3-beta, Km column.

normalized_value_unit_evidence: 43 uM normalizes to 0.043 mM, not exported 0.013 mM.

raw_value_unit_evidence: Table I reports Ap6A beta Km 43 uM.

row_label: Ap6A, isoform beta / hDIPP3-beta

enzyme: Diphosphoinositol polyphosphate phosphohydrolase 3-beta


enzyme_display_name: S-methyl-5'-thioadenosine deaminase

organism: Pseudomonas aeruginosa

substrate_name: adenosine

enzyme: S-methyl-5'-thioadenosine deaminase

substrate: adenosine


enzyme_display_name: nucleotide diphosphatase

substrate_name: dITP

column_label: Table I; row dITP; columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1).

normalized_value_unit_evidence: kcat 360 s^-1 from explicit paper cell; kcat_over_km 1160 s^-1 mM^-1 from explicit paper cell; km 0.31 mM from explicit paper cell

row_label: dITP

table_label: Table I

enzyme: nucleotide diphosphatase

substrate: dITP


substrate_name: ITP

column_label: Table I; row ITP; columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1).

normalized_value_unit_evidence: kcat 580 s^-1 from explicit paper cell; kcat_over_km 1140 s^-1 mM^-1 from explicit paper cell; km 0.51 mM from explicit paper cell

row_label: ITP

substrate: ITP


substrate_name: XTP

column_label: Table I; row XTP; columns Km (mM), kcat (s^-1), kcat/Km (10^3 M^-1 s^-1).

normalized_value_unit_evidence: kcat 640 s^-1 from explicit paper cell; kcat_over_km 1120 s^-1 mM^-1 from explicit paper cell; km 0.57 mM from explicit paper cell

row_label: XTP

substrate: XTP


enzyme_display_name: UniProt P96965

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

enzyme: UniProt P96965


organism: Pseudomonas putida

substrate_name: catechol

substrate: catechol


enzyme_display_name: exopolyphosphatase

organism: Trypanosoma brucei brucei

substrate_name: ADP

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

enzyme: exopolyphosphatase

substrate: ADP


substrate_name: ATP

substrate: ATP


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Thermococcus kodakarensis

substrate_name: D-fructose 6-phosphate

column_label: Official PMC full text Table 1 row Fru6P (at 170 mM ammonia), amination direction, reports kcat, Km, and kcat/Km.

normalized_value_unit_evidence: Km=1.10 mM; kcat=44.2 s^-1; kcat/Km=40.18181818181818 s^-1 mM^-1 from displayed kcat/Km ratio

row_label: Amination; Fru6P (at 170 mM ammonia)

table_label: PMC HTML Table 1: Kinetic properties of GlmD_Tk

enzyme: glucosamine-6-phosphate deaminase

substrate: D-fructose 6-phosphate


substrate_name: D-glucosamine 6-phosphate

column_label: Official PMC full text Table 1 row GlcN6P, deamination direction, reports kcat, Km, and kcat/Km.

normalized_value_unit_evidence: Km=0.339 mM; kcat=97.5 s^-1; kcat/Km=287.6106194690265 s^-1 mM^-1 from displayed kcat/Km ratio

row_label: Deamination; GlcN6P

substrate: D-glucosamine 6-phosphate


substrate_name: meta-ring fission intermediate

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

mutation_type: substitution

substrate: meta-ring fission intermediate


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


organism: Flavobacterium sp.

substrate_name: 2-hydroxy-5-methylmuconic semialdehyde

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

substrate: 2-hydroxy-5-methylmuconic semialdehyde


substrate_name: 2-hydroxymuconic semialdehyde

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

substrate: 2-hydroxymuconic semialdehyde


organism: Rhodococcus globerulus


substrate_name: D-Glucosamine 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H164C/C118S/C228S/C239S to reconstruct the assayed variant sequence.

substrate: D-Glucosamine 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S206C/C118S/C228S/C239S to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt A0ACD6B9C3

organism: Sphingobium sp. SYK-6

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

enzyme: UniProt A0ACD6B9C3


enzyme_display_name: Nudix hydrolase 7

organism: Arabidopsis thaliana

substrate_name: NADH

assay_conditions_summary: cofactor NADH

enzyme: Nudix hydrolase 7

substrate: NADH


substrate_name: ADP-ribose

substrate: ADP-ribose


enzyme_display_name: cyclohexane-1,3-dione hydrolase

organism: Clostridium sp.

enzyme: cyclohexane-1,3-dione hydrolase


organism: Janthinobacterium sp. J3


organism: Arthrobacter sp. YC-RL1


organism: Pseudomonas sp.


organism: Burkholderia xenovorans

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


organism: Metapseudomonas resinovorans

substrate_name: HOPDA (at pH 7.5 and 25 degrees Celsius)

assay_conditions_summary: pH 7.5; buffer 50 mM sodium phosphate

column_label: PMID 12619671 DOI 10.1016/S0006-291X(03)00375-9 Table 1; rows CarCCA10 / 6-Phenyl HODA and CarCCA10 / HODA; Km (uM) column.

normalized_value_unit_evidence: 6-Phenyl HODA Km normalizes to 0.00251 mM; HODA kinetic parameters are not determined.

raw_value_unit_evidence: Table 1 row CarCCA10 / 6-Phenyl HODA gives Km 2.51 uM; the separate HODA row reports ND for Km, kcat, and kcat/Km because of low activity.

row_label: CarCCA10 / 6-Phenyl HODA; CarCCA10 / HODA

table_label: Table 1. Kinetic parameters of native CarCCA10, ht-CarCCA10, and ht-CarCJ3


organism: Burkholderia cepacia


organism: Mycobacterium tuberculosis

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

source_databases_merged: sabio_rk skid uniprot


substrate_name: H2O; 3-Methylcatechol ring-fission product

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


organism: Cupriavidus necator

proof_lines:
isoenzyme HODHII
isoenzyme HODHI


proof_lines:
isoenzyme HODHI
isoenzyme HODHII


proof_lines: kcat is 2.14 sec(-1) for 6-phenyl-HODA (at 50 mM sodium phosphate, pH 7.5, 25 degrees Celsius).


organism: Comamonas testosteroni

substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli (strain K12)

substrate_name: 2-hydroxy-6-oxononadienedioate (at pH 8)

assay_conditions_summary: pH 8

proof_lines: kcat is 28 sec(-1) for hydrolase activity with 2-hydroxy-6-oxononadienedioate as substrate.


source_databases_merged: sabio_rk brenda uniprot


organism: Paraburkholderia xenovorans

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H265A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D237N to reconstruct the assayed variant sequence.


column_label: Table 4, HMSH row 2-HMS, columns KM, kcat, kcat/KM.

row_label: HMSH / 2-HMS

table_label: Table 4


column_label: Table 4, HMSH row HODA, columns KM, kcat, kcat/KM.

row_label: HMSH / HODA


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S112A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P47229 and applied mutation signature R188K with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, BphD block, variant row R188K; column KM (uM) = 2.0; column kcat (s^-1) = 0.009; column kcat/KM (M^-1 s^-1) = 2.8 x 10^3. captured primary segment: BphD R188K | KM 2.0 uM | kcat 0.009 s^-1 | kcat/KM 2.8 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2.0 uM; 1 uM is 1/1000 mM, so 2.0 / 1000 = 0.002 mM. kcat: printed Table 2 kcat cell 0.009 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.009 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2.8 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2800 / 1000 = 2.8 s^(-1)*mM^(-1). The catalog stores no catalytic-efficiency value for this measurement, so this pass reports the printed cell in the typed ratio provenance only and adds no kcat_over_km metric. Quotient disclosure for this row: 0.009 / 0.002 = 4.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, BphD block, variant row R188K: KM = 2.0 uM; kcat = 0.009 s^-1; printed kcat/KM = 2.8 x 10^3 M^-1 s^-1.

row_label: Table 2, BphD block, variant row R188K


column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, BphD block, enzyme row wild-type BphD; column KM (uM) = 2.0; column kcat (s^-1) = 6.5; column kcat/KM (M^-1 s^-1) = 3.3 x 10^6. captured primary segment: wild-type BphD | KM 2.0 uM | kcat 6.5 s^-1 | kcat/KM 3.3 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 2.0 uM; 1 uM is 1/1000 mM, so 2.0 / 1000 = 0.002 mM. kcat: printed Table 2 kcat cell 6.5 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 6.5 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 3.3 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3300000 / 1000 = 3300.0 s^(-1)*mM^(-1). The catalog stores no catalytic-efficiency value for this measurement, so this pass reports the printed cell in the typed ratio provenance only and adds no kcat_over_km metric. Quotient disclosure for this row: 6.5 / 0.002 = 3250.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, BphD block, enzyme row wild-type BphD: KM = 2.0 uM; kcat = 6.5 s^-1; printed kcat/KM = 3.3 x 10^6 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P47229 and applied mutation signature R188Q with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, BphD block, variant row R188Q; column KM (uM) = 28.2; column kcat (s^-1) = 0.016; column kcat/KM (M^-1 s^-1) = 5.7 x 10^2. captured primary segment: BphD R188Q | KM 28.2 uM | kcat 0.016 s^-1 | kcat/KM 5.7 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 28.2 uM; 1 uM is 1/1000 mM, so 28.2 / 1000 = 0.0282 mM. kcat: printed Table 2 kcat cell 0.016 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.016 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 5.7 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 570 / 1000 = 0.57 s^(-1)*mM^(-1). The catalog stores no catalytic-efficiency value for this measurement, so this pass reports the printed cell in the typed ratio provenance only and adds no kcat_over_km metric. Quotient disclosure for this row: 0.016 / 0.0282 = 0.5673758865248227 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, BphD block, variant row R188Q: KM = 28.2 uM; kcat = 0.016 s^-1; printed kcat/KM = 5.7 x 10^2 M^-1 s^-1.

row_label: Table 2, BphD block, variant row R188Q


organism: Pseudomonas putida

substrate_name: 3-methylcatechol ring-fission product

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H249A to reconstruct the assayed variant sequence.

substrate: 3-methylcatechol ring-fission product


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature C261A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row C261A; column KM (uM) = 4.2; column kcat (s^-1) = 12; column kcat/KM (M^-1 s^-1) = 2.9 x 10^6. captured primary segment: MhpC C261A | KM 4.2 uM | kcat 12 s^-1 | kcat/KM 2.9 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 4.2 uM; 1 uM is 1/1000 mM, so 4.2 / 1000 = 0.0042 mM. kcat: printed Table 2 kcat cell 12 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 12.0 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2.9 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2900000 / 1000 = 2900.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 12.0 / 0.0042 = 2857.1428571428573 s^-1 mM^-1, which is the value the catalog carries, and the printed catalytic-efficiency cell 2.9 x 10^6 M^-1 s^-1 is that same quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 2, MhpC block, variant row C261A: KM = 4.2 uM; kcat = 12 s^-1; printed kcat/KM = 2.9 x 10^6 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row C261A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature F173D with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row F173D; column KM (uM) = 10; column kcat (s^-1) = 0.26; column kcat/KM (M^-1 s^-1) = 2.6 x 10^4. captured primary segment: MhpC F173D | KM 10 uM | kcat 0.26 s^-1 | kcat/KM 2.6 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 10 uM; 1 uM is 1/1000 mM, so 10 / 1000 = 0.01 mM. kcat: printed Table 2 kcat cell 0.26 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.26 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2.6 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 26000 / 1000 = 26.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.26 / 0.01 = 26.0 s^-1 mM^-1, the same value as the printed catalytic-efficiency cell, so this row closes on its own printed cells.

raw_value_unit_evidence: Table 2, MhpC block, variant row F173D: KM = 10 uM; kcat = 0.26 s^-1; printed kcat/KM = 2.6 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row F173D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature F173G with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row F173G; column KM (uM) = 58; column kcat (s^-1) = 7.5; column kcat/KM (M^-1 s^-1) = 1.3 x 10^5. captured primary segment: MhpC F173G | KM 58 uM | kcat 7.5 s^-1 | kcat/KM 1.3 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 58 uM; 1 uM is 1/1000 mM, so 58 / 1000 = 0.058 mM. kcat: printed Table 2 kcat cell 7.5 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 7.5 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 1.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 130000 / 1000 = 130.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 7.5 / 0.058 = 129.3103448275862 s^-1 mM^-1, which is the value the catalog carries, and the printed catalytic-efficiency cell 1.3 x 10^5 M^-1 s^-1 is that same quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 2, MhpC block, variant row F173G: KM = 58 uM; kcat = 7.5 s^-1; printed kcat/KM = 1.3 x 10^5 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row F173G


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature N109A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row N109A; column KM (uM) = 4.0; column kcat (s^-1) = 0.13; column kcat/KM (M^-1 s^-1) = 3.3 x 10^4. captured primary segment: MhpC N109A | KM 4.0 uM | kcat 0.13 s^-1 | kcat/KM 3.3 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 4.0 uM; 1 uM is 1/1000 mM, so 4.0 / 1000 = 0.004 mM. kcat: printed Table 2 kcat cell 0.13 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.13 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 3.3 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 33000 / 1000 = 33.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.13 / 0.004 = 32.5 s^-1 mM^-1, against the printed catalytic-efficiency cell 33.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MhpC block, variant row N109A: KM = 4.0 uM; kcat = 0.13 s^-1; printed kcat/KM = 3.3 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row N109A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature N109H with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row N109H; column KM (uM) = 4.0; column kcat (s^-1) = 0.08; column kcat/KM (M^-1 s^-1) = 1.9 x 10^4. captured primary segment: MhpC N109H | KM 4.0 uM | kcat 0.08 s^-1 | kcat/KM 1.9 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 4.0 uM; 1 uM is 1/1000 mM, so 4.0 / 1000 = 0.004 mM. kcat: printed Table 2 kcat cell 0.08 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.08 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 1.9 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 19000 / 1000 = 19.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.08 / 0.004 = 20.0 s^-1 mM^-1, against the printed catalytic-efficiency cell 19.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MhpC block, variant row N109H: KM = 4.0 uM; kcat = 0.08 s^-1; printed kcat/KM = 1.9 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row N109H


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature R188K with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row R188K; column KM (uM) = 38; column kcat (s^-1) = 0.74; column kcat/KM (M^-1 s^-1) = 1.9 x 10^4. captured primary segment: MhpC R188K | KM 38 uM | kcat 0.74 s^-1 | kcat/KM 1.9 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 38 uM; 1 uM is 1/1000 mM, so 38 / 1000 = 0.038 mM. kcat: printed Table 2 kcat cell 0.74 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.74 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 1.9 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 19000 / 1000 = 19.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.74 / 0.038 = 19.473684210526315 s^-1 mM^-1, which is the value the catalog carries, and the printed catalytic-efficiency cell 1.9 x 10^4 M^-1 s^-1 is that same quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 2, MhpC block, variant row R188K: KM = 38 uM; kcat = 0.74 s^-1; printed kcat/KM = 1.9 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row R188K


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature R188Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row R188Q; column KM (uM) = 77; column kcat (s^-1) = 0.10; column kcat/KM (M^-1 s^-1) = 1.4 x 10^3. captured primary segment: MhpC R188Q | KM 77 uM | kcat 0.10 s^-1 | kcat/KM 1.4 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 77 uM; 1 uM is 1/1000 mM, so 77 / 1000 = 0.077 mM. kcat: printed Table 2 kcat cell 0.10 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.1 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 1.4 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1400 / 1000 = 1.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.1 / 0.077 = 1.2987012987012987 s^-1 mM^-1, against the printed catalytic-efficiency cell 1.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MhpC block, variant row R188Q: KM = 77 uM; kcat = 0.10 s^-1; printed kcat/KM = 1.4 x 10^3 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row R188Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P77044 and applied mutation signature W264G with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2: Steady-State Kinetic Parameters for MhpC and BphD Mutant Enzymes (Biochemistry 2006, volume 45, pages 12470-12479); printed column heads variant | KM (uM) | kcat (s^-1) | kcat/KM (M^-1 s^-1). Table 2, MhpC block, variant row W264G; column KM (uM) = 125; column kcat (s^-1) = 2.7; column kcat/KM (M^-1 s^-1) = 2.1 x 10^4. captured primary segment: MhpC W264G | KM 125 uM | kcat 2.7 s^-1 | kcat/KM 2.1 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 KM cell 125 uM; 1 uM is 1/1000 mM, so 125 / 1000 = 0.125 mM. kcat: printed Table 2 kcat cell 2.7 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 2.7 s^(-1). kcat/Km: printed Table 2 kcat/KM cell 2.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.7 / 0.125 = 21.6 s^-1 mM^-1, against the printed catalytic-efficiency cell 21.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, MhpC block, variant row W264G: KM = 125 uM; kcat = 2.7 s^-1; printed kcat/KM = 2.1 x 10^4 M^-1 s^-1.

row_label: Table 2, MhpC block, variant row W264G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S112C 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.

proof_lines: pH 7.5, 25°C, recombinant wild-type BphD, with 12940 mM methanol


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 3-Cl HOPDA: Km column 0.54 (0.02) uM, kcat column 0.0089 (0.0001) s^-1, kcat/Km x 10^-5 column 0.16 (0.01) M^-1 s^-1.

row_label: 3-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 5-Cl HOPDA: Km column 4.9 (0.1) uM, kcat column 1.53 (0.01) s^-1, kcat/Km x 10^-5 column 3.11 (0.05) M^-1 s^-1.

row_label: 5-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 8-Cl HOPDA: Km column 0.33 (0.02) uM, kcat column 2.10 (0.03) s^-1, kcat/Km x 10^-5 column 64 (3) M^-1 s^-1.

row_label: 8-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 9-Cl HOPDA: Km column 0.46 (0.03) uM, kcat column 3.9 (0.1) s^-1, kcat/Km x 10^-5 column 85 (4) M^-1 s^-1.

row_label: 9-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row 10-Cl HOPDA: Km column 0.13 (0.01) uM, kcat column 3.13 (0.04) s^-1, kcat/Km x 10^-5 column 246 (13) M^-1 s^-1.

row_label: 10-Cl HOPDA


column_label: Table III, Steady-state kinetic parameters of B. cepacia LB400 BphD with monochlorinated HOPDAs row HOPDA: Km column 0.19 (0.01) uM, kcat column 4.18 (0.03) s^-1, kcat/Km x 10^-5 column 225 (6) M^-1 s^-1.

row_label: HOPDA


enzyme_display_name: Nudix hydrolase 23, chloroplastic

substrate_name: FAD

assay_conditions_summary: cofactor FAD

enzyme: Nudix hydrolase 23, chloroplastic

substrate: FAD


enzyme_display_name: Nucleoside-triphosphatase THEP1

organism: Aquifex aeolicus (strain VF5)

assay_conditions_summary: buffer 25 uL; cofactor ATP

column_label: Abstract/Fig. 7 kinetic annotation for ATP; Km value 5.5 +/- 1.4 x 10^-6 M.

normalized_value_unit_evidence: 5.5 +/- 1.4 x 10^-6 M normalizes to 0.0055 mM, matching the export.

raw_value_unit_evidence: Paper reports Km = 5.5 +/- 1.4 x 10^-6 M for ATP.

row_label: ATP hydrolysis

table_label: Abstract and Fig. 7: aaTHEP1 hydrolyzes ATP and GTP obeying Michaelis-Menten equation

enzyme: Nucleoside-triphosphatase THEP1


substrate_name: GTP

column_label: Abstract/Fig. 7 kinetic annotation for GTP; Km value 45 +/- 25 x 10^-6 M.

normalized_value_unit_evidence: 45 +/- 25 x 10^-6 M normalizes to 0.045 mM, matching the export.

raw_value_unit_evidence: Paper reports Km = 45 +/- 25 x 10^-6 M for GTP.

row_label: GTP hydrolysis

substrate: GTP


column_label: Table 4, HMSH row HMMS, columns KM, kcat, kcat/KM.

row_label: HMSH / HMMS


column_label: Table 4, HMSH row HODA, columns KM, kcat, kcat/KM.

row_label: HMSH / HODA


column_label: Table 4, HMSH row 2-HMS, columns KM, kcat, kcat/KM.

row_label: HMSH / 2-HMS


enzyme_display_name: nucleoside-triphosphate phosphatase

organism: Bacteriophage phi-6

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
bacteriophage phi-6
P4
NTPase

enzyme: nucleoside-triphosphate phosphatase


substrate_name: UTP

substrate: UTP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H114A 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 H263A 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 S110A 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 S110G 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 S40A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


enzyme_display_name: m7GpppX diphosphatase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: m7GpppG (homodimer)

proof_lines: kcat is 0.012 sec(-1) with m7GpppG as substrate (homodimer). kcat is 0.0015 sec(-1) with m7GpppG as substrate (heterodimer). kcat is 0.0017 sec(-1) with m7GDP as substrate (homodimer). kcat is 0.0005 sec(-1) with m7GDP as substrate (heterod

enzyme: m7GpppX diphosphatase

substrate: m7GpppG (homodimer)


substrate_name: m7GDP (homodimer)

substrate: m7GDP (homodimer)


organism: Dyella ginsengisoli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148I to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M148A to reconstruct the assayed variant sequence.


enzyme_display_name: cyclohexane-1,2-dione hydrolase

organism: Azoarcus sp.

proof_lines:
cyclohexane-1,2-dione hydrolase
Azoarcus sp. strain 22Lin
cyclohexane-1,2-dione

source_databases_merged: brenda skid uniprot

enzyme: cyclohexane-1,2-dione hydrolase


column_label: PMC2804191 HTML lines 1535-1560 define Table 2 columns and units; lines 1564-1567 give row HOPDA: Km 8 (1) uM, kcat 0.066 (0.005) s^-1, kcat/Km 9 (1) mM^-1 s^-1.

normalized_value_unit_evidence: Km 0.008 mM; kcat 0.066 s^-1; kcat/Km 9 s^-1*mM^-1 from the primary Table 2 HOPDA row. Exported kcat/Km is 8.25 s^-1*mM^-1 and does not equal the primary paper value.

table_label: Table 2: Steady-state kinetic parameters of HsaD with HOPDA, HOPODA, and DSHA


column_label: PMC2804191 HTML lines 1535-1560 define Table 2 columns and units; lines 1570-1573 give row HOPODA: Km 310 (70) uM, kcat 0.33 (0.06) s^-1, kcat/Km 1.06 (0.06) mM^-1 s^-1.

normalized_value_unit_evidence: Km 0.310 mM; kcat 0.33 s^-1; kcat/Km 1.06 s^-1*mM^-1 from the primary Table 2 HOPODA row. Exported kcat/Km is 1.0645161290322582 s^-1*mM^-1 and does not exactly equal the primary paper value.

row_label: HOPODA


enzyme_display_name: Nucleotide triphosphate diphosphatase NUDT15

organism: Mus musculus

column_label: Abstract reports mMTH2 protein hydrolyzes 8-oxo-dGTP to 8-oxo-dGMP, with Km of 32 microM.

raw_value_unit_evidence: Km raw_value=32 microM raw_unit=microM

row_label: Mouse MTH2 / 8-oxo-dGTP

table_label: PubMed XML abstract PMID 12767940


enzyme: Nucleotide triphosphate diphosphatase NUDT15


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148L to reconstruct the assayed variant sequence.


enzyme_display_name: diadenosine hexaphosphate hydrolase (ATP-forming)


enzyme: diadenosine hexaphosphate hydrolase (ATP-forming)


organism: Saccharomyces cerevisiae

substrate_name: 7-methylguanosine 5'-diphosphate

assay_conditions_summary: pH 7; 303.15 K; buffer 10 mM Tris-HCl pH 7

column_label: Table 2, Dcs1 homodimer row for m7GDP, reports KM 0.26 uM, kcat 1.7 x 10^-3 s^-1, and independently printed kcat/KM 6.5 x 10^3 M^-1 s^-1.

row_label: Dcs1 homodimer / m7GDP (text extraction renders m7Gpp)

table_label: Primary article PDF page 5 / printed page 374, Table 2

substrate: 7-methylguanosine 5'-diphosphate


column_label: Table 2, Dcs1 homodimer row for m7GpppG, reports KM 0.14 uM, kcat 12.0 x 10^-3 s^-1, and independently printed kcat/KM 8.6 x 10^4 M^-1 s^-1.

row_label: Dcs1 homodimer / m7GpppG


substrate_name: dTTP

column_label: Table 1 reports dTTP Km 0.09 mM, Vmax 0.06 mM s^-1, kcat 43 s^-1, kcat/Km 503 mM^-1 s^-1, N 2.2; KM and kcat match, but kcat/Km differs from the current export

normalized_value_unit_evidence: KM normalized_value=0.09 normalized_unit=mM; kcat normalized_value=43 normalized_unit=s^-1; kcat_over_km normalized_value=503 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=477.77777777777777 s^-1*mM^-1

raw_value_unit_evidence: KM raw_value=0.09 raw_unit=mM; kcat raw_value=43 raw_unit=s^-1; kcat_over_km raw_value=503 raw_unit=s^-1*mM^-1 for dTTP

row_label: YhdE dTTP row; KM, kcat, and kcat/KM columns

table_label: PMID 25658941 PMC HTML Table 1

substrate: dTTP


column_label: Table 1 reports UTP Km 0.5 mM, Vmax 0.14 mM s^-1, kcat 95 s^-1, kcat/Km 191 mM^-1 s^-1, N 1.9; KM and kcat match, but kcat/Km differs from the current export

normalized_value_unit_evidence: KM normalized_value=0.5 normalized_unit=mM; kcat normalized_value=95 normalized_unit=s^-1; kcat_over_km normalized_value=191 normalized_unit=s^-1*mM^-1; current_export_kcat_over_km=190 s^-1*mM^-1

raw_value_unit_evidence: KM raw_value=0.5 raw_unit=mM; kcat raw_value=95 raw_unit=s^-1; kcat_over_km raw_value=191 raw_unit=s^-1*mM^-1 for UTP

row_label: YhdE UTP row; KM, kcat, and kcat/KM columns


enzyme_display_name: GTP cyclohydrolase II

organism: Meyerozyma guilliermondii

enzyme: GTP cyclohydrolase II


enzyme_display_name: Name not preserved

organism: Thermus thermophilus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ADP

proof_lines:
pH 7.5, 25°C
pH 9.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5

source_databases_merged: brenda skid

enzyme: Name not preserved


assay_conditions_summary: pH 9; 298.15 K; cofactor FAD


assay_conditions_summary: pH 7.5; 298.15 K; cofactor FAD


enzyme_display_name: S-adenosylhomocysteine deaminase

organism: Thermotoga maritima

substrate_name: S-Adenosyl-L-homocysteine

column_label: Table 2 row S-adenosyl-L-homocysteine gives Km 210 +/- 40 uM, kcat 12.2 +/- 0.8 s^-1, and kcat/Km 5.8 x 10^4 M^-1 s^-1; Figure S3 confirms the same SAH kinetic plot at pH 8.0 and 30 C.

row_label: S-adenosyl-L-homocysteine

table_label: Table 2: Docking ranks and Tm0936 catalytic constants for five predicted substrates

enzyme: S-adenosylhomocysteine deaminase

substrate: S-Adenosyl-L-homocysteine


enzyme_display_name: UniProt A6G7B1

organism: Plesiocystis pacifica

smiles: C(CBr)Br

enzyme: UniProt A6G7B1


smiles: CCCCCCBr


smiles: CCCBr


smiles: CC(CBr)Br


smiles: CCCCCCCBr


smiles: CCCCBr


smiles: CCCCCBr


enzyme_display_name: UniProt Q6DND9

organism: Lyngbya majuscula

smiles: CCCCCl

enzyme: UniProt Q6DND9


smiles: CCCCI


smiles: C(CC#N)CBr


smiles: CCCI


enzyme_display_name: UniProt Q9A919

organism: Caulobacter vibrioides

smiles: CCCCCCCl

enzyme: UniProt Q9A919


smiles: C(CCCl)CCCl


smiles: C(CBr)CBr


enzyme_display_name: atrazine chlorohydrolase

organism: Arthrobacter sp.

substrate_name: Atrazine

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

enzyme: atrazine chlorohydrolase

substrate: Atrazine


enzyme_display_name: dCTP deaminase, dUMP-forming

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

substrate_name: dUTP (at 60 degrees Celsius)

column_label: PMID 12538648 dUTP diphosphatase kinetic evidence, dUTP row/segment, Km = 263 +/- 64 uM at 60 deg C.

raw_value_unit_evidence: The paper reports dUTP diphosphatase Km = 263 +/- 64 uM.

row_label: dUTP diphosphatase reaction

table_label: Table III and dUTP diphosphatase kinetic prose for MjDCD-DUT

enzyme: dCTP deaminase, dUMP-forming

substrate: dUTP (at 60 degrees Celsius)


organism: Methanocaldococcus jannaschii

substrate_name: dCTP

source_databases_merged: brenda uniprot

substrate: dCTP


enzyme_display_name: GTP cyclohydrolase-2

organism: Escherichia coli

enzyme: GTP cyclohydrolase-2


organism: Haematococcus lacustris

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


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


proof_lines: more than 0.153 mM. AtzA wild type, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216S/T217A/T219P/A220F/D250G, site-directed mutagenesis, AtzA-variant 357, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216A/T217D/T219E/A220A/D250D, site-directed mutagenesis, AtzA-variant 288, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216G/T217D/T219A/A220V/D250W, site-directed mutagenesis, AtzA-variant 305, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216Y/T217D/T219Y/A220H/D250V, site-directed mutagenesis, AtzA-variant 422, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216S/T217D/T219V/A220H/D250G, site-directed mutagenesis, AtzA-variant 297, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216H/T217A/T219E/A220S/D250S, site-directed mutagenesis, AtzA-variant 662, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216A/T217S/T219H/A220G/D250Y, site-directed mutagenesis, AtzA-variant 431, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216S/T217D/T219G/A220S/D250D, site-directed mutagenesis, AtzA-variant 841, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216G/T217D/T219G/A220H/D250G, site-directed mutagenesis, AtzA-variant 430, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216G/T217D/T219G/A220H/D250D, site-directed mutagenesis, AtzA-variant 734, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: A216Y/T217D/T219T/A220H/D250E, site-directed mutagenesis, AtzA best variant consensus, kinetic data obtained using 4.6 to 153 microM atrazine and 10 nM enzyme


proof_lines: AtzA wild-type, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216S/T217A/T219P/A220F/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: T217D/T219E, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216G/T217D/T219A/A220V/D250W, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216Y/T217D/T219Y/A220H/D250V, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216S/T217D/T219V/A220H/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216H/T217A/T219E/A220S/D250S, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: T217S/T219H/A220G/D250Y, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216S/T217D/T219G/A220S, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216G/T217D/T219G/A220H/D250G, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216G/T217D/T219G/A220H/D250D, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


proof_lines: A216Y/T217D/A220H/D250E, AtzA mutant, substrate concentration 153 microM, enzyme concentration 10 nM, measuring absorbance of atrazine after reaction with pyridine at 436 nm


enzyme_display_name: haloalkane dehalogenase

enzyme: haloalkane dehalogenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M148Y 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.


organism: Paenarthrobacter aurescens

proof_lines: mutant R325S, pH and temperature not specified in the publication


proof_lines: mutant E241Q, pH and temperature not specified in the publication


substrate_name: ametryn

substrate: ametryn


proof_lines: wild-type enzyme, pH 7.0, temperature not specified in the publication


proof_lines: mutant R325, pH and temperature not specified in the publicationS


organism: Alloalcanivorax dieselolei

assay_conditions_summary: pH 8.6; buffer pH 8

column_label: Table 2 row 1-Chlorobutane / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).

table_label: Table 2


column_label: Table 2 row 1,3-Dibromopropane / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


column_label: Table 2 row 1,2-Dibromoethane / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


smiles: C=C(CCl)Cl

column_label: Table 2 row 2,3-Dichloroprop-1-ene / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


column_label: Table 2 row 4-bromobutanenitrile (synonym: 4-bromobutyronitrile) / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


smiles: CC(=C)CCl

column_label: Table 2 row 3-chloro-2-methylprop-1-ene / HLD DadB; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).


enzyme_display_name: (R)-2-haloacid dehalogenase

organism: Agrobacterium sp.

enzyme: (R)-2-haloacid dehalogenase


enzyme_display_name: S-methyl-5'-thioadenosine deaminase

column_label: Table 2 row 5-Methyl-thioadenosine gives Km 44 +/- 4 uM, kcat 7.2 +/- 0.2 s^-1, and kcat/Km 1.4 x 10^5 M^-1 s^-1; Figure S3 confirms the same MTA kinetic plot at pH 8.0 and 30 C.

enzyme: S-methyl-5'-thioadenosine deaminase


enzyme_display_name: 4-chlorobenzoate dehalogenase

enzyme: 4-chlorobenzoate dehalogenase


organism: Strongylocentrotus purpuratus

proof_lines: pH 8.6, 37°C, recombinant His-tagged enzyme


enzyme_display_name: 4-chlorobenzoyl-CoA dehalogenase

organism: Pseudomonas sp.

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature G114A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM K+Hepes; cofactor CoA

column_label: Table 3, enzyme row 'G114A'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.002 and column 'Km (uM)' = 110. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.002 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.002 s^(-1). Km: printed Table 3 cell 110 uM; 110 / 1000 = 0.11 mM; the paper value is 0.11 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 0.01818181818181818 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.002 / 0.11 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'G114A': kcat = 0.002 s-1; Km = 110 uM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row G114A

table_label: Table 3: Kinetic Constants (kcat and Km) for Wild-Type and Mutant 4-CBA-CoA Dehalogenase Catalysis and Dissociation Constants (Kd) and/or Inhibition Constants (Ki) for 4-MeBA-CoA, 4-HBA-CoA, and CoA with Wild-Type and Mutant 4-CBA-CoA Dehalogenase (Measured at pH 7.5 and 25 °C in 50 mM K+Hepes Buffer) (Biochemistry 2001, 40(51):15684-15692)

enzyme: 4-chlorobenzoyl-CoA dehalogenase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G113A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature F64A to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'F64A'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.03 and column 'Km (uM)' = 5.2. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.03 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.03 s^(-1). Km: printed Table 3 cell 5.2 uM; 5.2 / 1000 = 0.0052 mM; the paper value is 0.0052 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 5.769230769230769 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.03 / 0.0052 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, enzyme row 'F64A': kcat = 0.03 s-1; Km = 5.2 uM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, enzyme row F64A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R257L to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R257L'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.14 and column 'Km (uM)' = 70. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.14 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.14 s^(-1). Km: printed Table 1 cell 70 uM; 70 / 1000 = 0.07 mM; the paper value is 0.07 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 2.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.14 / 0.07 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R257L': kcat = 0.14 s-1; Km = 70 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R257L

table_label: Table 1: Kinetic Constants (kcat and Km) for Wild-Type and Mutant 4-CBA-CoA Dehalogenase Catalysis and Dissociation Constants (Kd) and/or Inhibition Constants (Ki) for 4-MeBA-CoA, 4-HBA-CoA, and CoA with Wild-Type and Mutant 4-CBA-CoA Dehalogenase (Measured at pH 7.5 and 25 °C in 50 mM K+Hepes Buffer) (Biochemistry 2001, 40(51):15684-15692)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R24L to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R24L'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.33 and column 'Km (uM)' = 41. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.33 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.33 s^(-1). Km: printed Table 1 cell 41 uM; 41 / 1000 = 0.041 mM; the paper value is 0.041 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 8.048780487804878 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.33 / 0.041 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R24L': kcat = 0.33 s-1; Km = 41 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R24L


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R67K to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R67K'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.38 and column 'Km (uM)' = 6.9. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.38 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.38 s^(-1). Km: printed Table 1 cell 6.9 uM; 6.9 / 1000 = 0.0069 mM; the paper value is 0.0069 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 55.072463768115945 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.38 / 0.0069 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R67K': kcat = 0.38 s-1; Km = 6.9 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R67K


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R257K to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R257K'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.55 and column 'Km (uM)' = 5.8. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.55 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.55 s^(-1). Km: printed Table 1 cell 5.8 uM; 5.8 / 1000 = 0.0058 mM; the paper value is 0.0058 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 94.82758620689657 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.55 / 0.0058 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R257K': kcat = 0.55 s-1; Km = 5.8 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R257K


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5JTM5 and applied mutation signature R24K to reconstruct the assayed variant sequence.

column_label: Table 1, enzyme row 'R24K'; under the group head '4-CBA-CoA', column 'kcat (s-1)' = 0.95 and column 'Km (uM)' = 21. The remaining columns of the same row stand under the group heads '4-MeBA-CoA' and '4-HBA-CoA' and hold Ki or Kd ligand constants. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.95 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 0.95 s^(-1). Km: printed Table 1 cell 21 uM; 21 / 1000 = 0.021 mM; the paper value is 0.021 mM. kcat/Km: neither Table 1 nor Table 3 carries a kcat/Km column, so the paper value 45.238095238095234 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.95 / 0.021 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, enzyme row 'R24K': kcat = 0.95 s-1; Km = 21 uM; Table 1 prints no kcat/Km cell for this row.

row_label: Table 1, enzyme row R24K


enzyme_display_name: Haloalkane dehalogenase

organism: Sphingobium indicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S)

proof_lines: kcat is 0.98 sec(-1) with 1-chlorobutane as substrate.

enzyme: Haloalkane dehalogenase


smiles: C(CBr)Cl


smiles: CC(C)CBr


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G113S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A112V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y65D to reconstruct the assayed variant sequence.


organism: Agrobacterium tumefaciens

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

smiles: C(CCl)CCl


column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1-Chlorohexane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).

normalized_value_unit_evidence: kcat=0.039 s^-1; Km-like K0.5=0.07 mM; kcat_over_km table value=0.58 s^-1 mM^-1, consistent with expected 0.557142857142857 from rounded K0.5/kcat cells.

table_label: Table 1. Kinetic characteristics of DatA with six halogenated substrates


smiles: CCCCCCI

column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1-Iodohexane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).

normalized_value_unit_evidence: kcat=0.26 s^-1; Km-like K0.5=0.63 mM; kcat_over_km table value=0.42 s^-1 mM^-1, consistent with expected 0.41269841269841273 from rounded K0.5/kcat cells.


smiles: C(CI)CI

column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1,3-Diiodopropane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).


column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1,3-Dibromopropane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).

normalized_value_unit_evidence: kcat=1.47 s^-1; Km-like K0.5=2.15 mM; kcat_over_km table value=0.69 s^-1 mM^-1, consistent with expected 0.6837209302325582 from rounded K0.5/kcat cells.


smiles: CCCCCCBr

column_label: PMC HTML Table 1 and Europe PMC PDF text lines 110-123 report row 1-Bromohexane columns K0.5 (mM), kcat (s^-1), and kcat/K0.5 (s^-1 mM^-1).

normalized_value_unit_evidence: kcat=1.7 s^-1; Km-like K0.5=0.14 mM; kcat_over_km table value=12.20 s^-1 mM^-1, consistent with expected 12.14285714285714 from rounded K0.5/kcat cells.


organism: Ancylobacter aquaticus

smiles: C(CCl)Cl

assay_conditions_summary: pH 9

proof_lines: GJ10, calculated from rate constants for four-steps reaction mechanism


organism: Xanthobacter autotrophicus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F172W to reconstruct the assayed variant sequence.

proof_lines: GJ10, F172W mutant, calculated from rate constants for four-steps reaction mechanism


smiles: C(CBr)Br


organism: Mycolicibacterium rhodesiae


organism: Rhodococcus rhodochrous

smiles: C(CBr)O


smiles: CCCCCl


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W175Y to reconstruct the assayed variant sequence.

column_label: PMID 9790663 DOI 10.1021/bi9815187 Table 3; substrate block 1,2-dibromoethane; row Trp175Tyr; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row 1,2-dibromoethane Trp175Tyr: Km 0.06 mM; kcat 5.0 s^-1; kcat/Km 85 mM^-1 s^-1.

row_label: 1,2-dibromoethane / Trp175Tyr

table_label: Table 3. Halide-Binding and Steady-State Activity Parameters of Purified Wild-Type and Trp175Tyr Haloalkane Dehalogenase for DBE and DCE at pH 8.2 and 30 C


column_label: PMID 9790663 DOI 10.1021/bi9815187 Table 3; substrate block 1,2-dichloroethane; row Trp175Tyr; columns Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row 1,2-dichloroethane Trp175Tyr: Km 2.85 mM; kcat 0.33 s^-1; kcat/Km 0.1 mM^-1 s^-1.

row_label: 1,2-dichloroethane / Trp175Tyr


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y109W to reconstruct the assayed variant sequence.

proof_lines: below, recombinant mutant Y109W, pH 8.6, 37°C


smiles: CCCCBr


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H90Q to reconstruct the assayed variant sequence.

proof_lines: multiple turnovers, mutant H90Q, pH 7.5, 25°C

proof_lines: single turnover, mutant H90Q, pH 7.5, 25°C


organism: Yarrowia lipolytica

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

smiles: CCCCCCCCCCBr


smiles: CCCCCCCCCCCCBr


smiles: CCCBr


substrate_name: bis(2-chloroethyl) ether

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

smiles: C(CCl)OCCCl

proof_lines: 37°C, pH 8.2, enzyme multi-PEGylated with the thiosuccinimido butylamine linker

proof_lines: 37°C, pH 8.2, enzyme mono-PEGylated with the thiosuccinimido butylamine linker

proof_lines: inulin-conjugated enzyme, at pH 7.4 and 37°C

substrate: bis(2-chloroethyl) ether


organism: uncultured marine bacterium

smiles: C(CBr)CBr

proof_lines: pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E232G to reconstruct the assayed variant sequence.


organism: Pseudomonas putida

substrate_name: Monochloroacetate

proof_lines: pH 7.5, D-2-haloacid dehalogenase subtype

substrate: Monochloroacetate


substrate_name: 1-Chloropropane; H2O

substrate: 1-Chloropropane; H2O


proof_lines: enzyme in 40% (v/v) DSMO, in the absence of poly(allylamine hydrochloride), at pH 8.0 and 30°C

proof_lines: enzyme in 40% (v/v) DSMO, poly(allylamine hydrochloride):enzyme ratio of 4:1, at pH 8.0 and 30°C

proof_lines: enzyme in 40% (v/v) DSMO, poly(allylamine hydrochloride):enzyme ratio of 8:1, at pH 8.0 and 30°C


organism: Sphingobium sp.

substrate_name: beta-hexachlorocyclohexane

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature I253M to reconstruct the assayed variant sequence.

substrate: beta-hexachlorocyclohexane


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature V134I/H247A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 30°C, recombinant mutant V134I/H247A


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H247A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature T81A 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.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H247A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V134I/H247A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I253M to reconstruct the assayed variant sequence.


organism: Sphingomonas paucimobilis

substrate_name: H2O; 1-Chlorobutane

substrate: H2O; 1-Chlorobutane


substrate_name: Unknown

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R24K with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

substrate: Unknown


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

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ADP

proof_lines: kcat is 11 sec(-1) with atrazine as substrate.


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


assay_conditions_summary: cofactor CoA

proof_lines:
multiple turnovers
single turnover


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R257L with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R67K with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R24L with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G114A to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: wild-type enzyme, pH 7.5, 25°C, in presence of 1 mM 5'-ADP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G113A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R257K with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F64P with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines:
mutant F64P, pH 7.5, 25°C
below, mutant F64P, pH 7.5, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G113N to reconstruct the assayed variant sequence.


substrate_name: H2O; 4-Chlorobenzoyl-CoA

substrate: H2O; 4-Chlorobenzoyl-CoA


assay_conditions_summary: cofactor ADP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L288A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N203A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V51F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L288I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L288V to reconstruct the assayed variant sequence.


column_label: Primary measurement evidence: evidence location type: table note; evidence location label: article page 1108 unnumbered kinetic-parameter table; measurement identity label: wild-type AtzA-AD1; atrazine; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 100 mM Tris-HCl pH 7.2; atrazine 4.6-140 uM; 25 C; 10 min; HPLC; captured primary segment: wild-type AtzA-AD1 values were Km 146 +/- 10 uM, kcat 1.6 +/- 0.1 s^-1, and kcat/Km 1.1x10^4 +/- 0.1x10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km 0.146 mM; kcat 1.6 s^-1; exact quotient of the printed point values 1.6/0.146 = 10.958904109589042 s^-1 mM^-1; the table independently prints the rounded efficiency 11 +/- 1 s^-1 mM^-1.

raw_value_unit_evidence: Page 1108 table note reports wild-type AtzA-AD1 Km 146 +/- 10 uM, kcat 1.6 +/- 0.1 s^-1, and kcat/Km 1.1x10^4 +/- 0.1x10^4 s^-1 M^-1.

row_label: Wild-type AtzA-AD1 values in table note

table_label: Page 1108 unnumbered table: Mutation sites, specific activity, and kinetic parameters of the variants relative to wild type


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

column_label: Table 1; row 18; compound 2-bromoacetamide; column log Km (mM); cell 1.30

raw_value_unit_evidence: Table 1 row 18 / 2-bromoacetamide: log Km (mM)=1.30

row_label: 18 / 2-bromoacetamide


substrate_name: epichlorohydrin

column_label: Table 1; row 13; compound epichlorohydrine; column log Km (mM); cell 1.68

raw_value_unit_evidence: Table 1 row 13 / epichlorohydrine: log Km (mM)=1.68

row_label: 13 / epichlorohydrine

substrate: epichlorohydrin


substrate_name: Dichloromethane

smiles: C(Cl)Cl

column_label: Table 1; row 5; compound dichloromethane; column log Km (mM); cell 2.00

raw_value_unit_evidence: Table 1 row 5 / dichloromethane: log Km (mM)=2.00

row_label: 5 / dichloromethane

substrate: Dichloromethane


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

column_label: Table 1; row 17; compound 2-chloroacetamide; column log Km (mM); cell 2.00

raw_value_unit_evidence: Table 1 row 17 / 2-chloroacetamide: log Km (mM)=2.00

row_label: 17 / 2-chloroacetamide


smiles: C(CCl)O

column_label: Table 1; row 11; compound 2-chloroethanol; column log Km (mM); cell 2.60

raw_value_unit_evidence: Table 1 row 11 / 2-chloroethanol: log Km (mM)=2.60

row_label: 11 / 2-chloroethanol


column_label: Table 1; row 3; compound 1-bromobutane; column log Km (mM); cell -1.22

raw_value_unit_evidence: Table 1 row 3 / 1-bromobutane: log Km (mM)=-1.22

row_label: 3 / 1-bromobutane


column_label: Table 1; row 4; compound 1-bromohexane; column log Km (mM); cell -0.52

raw_value_unit_evidence: Table 1 row 4 / 1-bromohexane: log Km (mM)=-0.52

row_label: 4 / 1-bromohexane


smiles: C(C#N)Br

column_label: Table 1; row 16; compound 2-bromoacetonitrile; column log Km (mM); cell -0.31

raw_value_unit_evidence: Table 1 row 16 / 2-bromoacetonitrile: log Km (mM)=-0.31

row_label: 16 / 2-bromoacetonitrile


smiles: CC(CBr)Br

column_label: Table 1; row 10; compound 1,2-dibromopropane; column log Km (mM); cell 0.11

raw_value_unit_evidence: Table 1 row 10 / 1,2-dibromopropane: log Km (mM)=0.11

row_label: 10 / 1,2-dibromopropane


smiles: CCCCCCCl

column_label: Table 1; row 2; compound 1-chlorohexane; column log Km (mM); cell 0.15

raw_value_unit_evidence: Table 1 row 2 / 1-chlorohexane: log Km (mM)=0.15

row_label: 2 / 1-chlorohexane


substrate_name: epibromohydrine

column_label: Table 1; row 14; compound epibromohydrine; column log Km (mM); cell 0.34

raw_value_unit_evidence: Table 1 row 14 / epibromohydrine: log Km (mM)=0.34

row_label: 14 / epibromohydrine

substrate: epibromohydrine


substrate_name: Dibromomethane

smiles: C(Br)Br

column_label: Table 1; row 7; compound dibromomethane; column log Km (mM); cell 0.38

raw_value_unit_evidence: Table 1 row 7 / dibromomethane: log Km (mM)=0.38

row_label: 7 / dibromomethane

substrate: Dibromomethane


smiles: C(C#N)Cl

column_label: Table 1; row 15; compound 2-chloroacetonitrile; column log Km (mM); cell 0.80

raw_value_unit_evidence: Table 1 row 15 / 2-chloroacetonitrile: log Km (mM)=0.80

row_label: 15 / 2-chloroacetonitrile


smiles: C(CBr)O

column_label: Table 1; row 12; compound 2-bromoethanol; column log Km (mM); cell 1.04

raw_value_unit_evidence: Table 1 row 12 / 2-bromoethanol: log Km (mM)=1.04

row_label: 12 / 2-bromoethanol


smiles: CC(CCl)Cl

column_label: Table 1; row 9; compound 1,2-dichloropropane; column log Km (mM); cell 1.11

raw_value_unit_evidence: Table 1 row 9 / 1,2-dichloropropane: log Km (mM)=1.11

row_label: 9 / 1,2-dichloropropane


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L288V to reconstruct the assayed variant sequence.


proof_lines:
Pseudomonas sp. CBS-3
4-chlorobenzoyl-CoA dehalogenase


proof_lines:
4-iodobenzoyl-CoA
1.1 s-1
Pseudomonas sp. CBS-3


proof_lines:
4-bromobenzoyl-CoA
1.4 s-1
Pseudomonas sp. CBS-3


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

substrate_name: S-adenosyl-L-homocysteine

assay_conditions_summary: pH 8

column_label: Table 2 row S-adenosyl-L-homocysteine, column Km (uM), gives 210 +/- 40 uM; Figure S3 repeats Km=(0.21 +/- 0.04) mM for SAH.

raw_value_unit_evidence: Km raw=210 +/- 40 uM; Table 2 also gives kcat 12.2 +/- 0.8 s^-1 and kcat/Km 5.8 x 10^4 M^-1 s^-1 for the same row.

row_label: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


smiles: C(C(CCl)Cl)Cl

column_label: Table 1; row 1,2,3-trichloropropane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=2.2 mM; kcat=0.08 s^-1; printed kcat/Km=0.036 s^-1 mM^-1; exported kcat/Km=0.03636363636363636 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1,2,3-trichloropropane; columns: kcat=0.08 s^-1; Km=2.2 mM; kcat/Km=36 M^-1 s^-1.

table_label: Table 1


smiles: CCCCl

column_label: Table 1 row 1-chloropropane, columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table row 1-chloropropane reports kcat 0.48 s^-1, Km 1.0 mM, kcat/Km 480 M^-1 s^-1.

table_label: Table 1. Steady-State Activity Parameters of Purified DhaA at pH 9.4 and 30 C, PMID 12834356


smiles: C(CCl)CCl

column_label: Table 1; row 1,3-dichloropropane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=0.63 mM; kcat=1.3 s^-1; printed kcat/Km=2.0 s^-1 mM^-1; exported kcat/Km=2.0634920634920637 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1,3-dichloropropane; columns: kcat=1.3 s^-1; Km=0.63 mM; kcat/Km=2000 M^-1 s^-1.


column_label: Table 1; row 1,2-dibromopropane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=1.0 mM; kcat=2.3 s^-1; printed kcat/Km=2.3 s^-1 mM^-1; exported kcat/Km=2.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1,2-dibromopropane; columns: kcat=2.3 s^-1; Km=1.0 mM; kcat/Km=2300 M^-1 s^-1.


column_label: Table 1 row 1,3-dibromopropane, columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table row 1,3-dibromopropane reports kcat 2.7 s^-1, Km 0.005 mM, kcat/Km 540000 M^-1 s^-1.


smiles: CCCBr

column_label: Table 1; row 1-bromopropane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=0.6 mM; kcat=2.7 s^-1; printed kcat/Km=4.5 s^-1 mM^-1; exported kcat/Km=4.500000000000001 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1-bromopropane; columns: kcat=2.7 s^-1; Km=0.6 mM; kcat/Km=4500 M^-1 s^-1.


smiles: C(CO)CBr

column_label: Table 1; row 3-bromo-1-propanol; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=3.3 mM; kcat=3.0 s^-1; printed kcat/Km=0.91 s^-1 mM^-1; exported kcat/Km=0.9090909090909092 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 3-bromo-1-propanol; columns: kcat=3.0 s^-1; Km=3.3 mM; kcat/Km=910 M^-1 s^-1.


smiles: C(C(CBr)Br)Br

column_label: Table 1 row 1,2,3-tribromopropane, columns kcat (s^-1), Km (mM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table row 1,2,3-tribromopropane reports kcat 3.6 s^-1, Km 0.3 mM, kcat/Km 12000 M^-1 s^-1.


smiles: C(CBr)Br

column_label: Table 1; row 1,2-dibromoethane; kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized Table 1 values: Km=4.0 mM; kcat=14.3 s^-1; printed kcat/Km=3.6 s^-1 mM^-1; exported kcat/Km=3.575 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 1,2-dibromoethane; columns: kcat=14.3 s^-1; Km=4.0 mM; kcat/Km=3600 M^-1 s^-1.


enzyme_display_name: glucosamine-6-phosphate deaminase

organism: Bacillus subtilis

substrate_name: D-Glucosamine 6-phosphate

column_label: Official JBC full-text visible article, abstract and kinetic analysis prose for BsuNagB

raw_value_unit_evidence: BsuNagB kcat 28 s-1; Km(app) 0.13 mM; kinetic text kcat = 28 +/- 6 s-1 and Km(GlcN-6-P) = 0.13 +/- 0.02 mM

row_label: BsuNagB monomeric glucosamine-6-phosphate deaminase; GlcN-6-P

table_label: Official JBC full-text visible prose

enzyme: glucosamine-6-phosphate deaminase

substrate: D-Glucosamine 6-phosphate


enzyme_display_name: 2-aminomuconate deaminase

organism: Ectopseudomonas oleovorans

enzyme: 2-aminomuconate deaminase


organism: Escherichia coli

substrate_name: alpha-D-glucosamine 6-phosphate

substrate: alpha-D-glucosamine 6-phosphate


organism: Psychrobacter cryohalolentis

smiles: CCCCBr


smiles: C(CBr)CBr


organism: Shewanella oneidensis


organism: Staphylococcus aureus


enzyme_display_name: 4-chlorobenzoyl coenzyme A dehalogenase-2

organism: Arthrobacter sp

substrate_name: 4-iodobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)

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

assay_conditions_summary: pH 7.2; buffer 20 mM phosphate; cofactor CoA

proof_lines:
Arthrobacter sp. strain TM-1
4-chlorobenzoyl CoA dehalogenase
4-CBCoA


substrate_name: 4-bromobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)

enzyme: 4-chlorobenzoyl coenzyme A dehalogenase-2


substrate_name: 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)

assay_conditions_summary: pH 7.5; 303.15 K; buffer 20 mM phosphate; cofactor CoA


substrate_name: 4-fluorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


enzyme_display_name: 4-chlorobenzoyl coenzyme A dehalogenase-1

substrate: 4-iodobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


enzyme: 4-chlorobenzoyl coenzyme A dehalogenase-1

substrate: 4-bromobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


substrate: 4-chlorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


substrate: 4-fluorobenzoyl-CoA (at 30 degrees Celsius, in 20 mM phosphate buffer, pH 7.2)


organism: Methylobacterium nodulans


organism: Methylobacterium radiotolerans


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 1

organism: Homo sapiens


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase DDP1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Rattus norvegicus

column_label: The abstract reports rat hepatic DIPP cleaves PP-InsP5 with Km = 340 nM.

raw_value_unit_evidence: Km raw_value=340 nM raw_unit=nM

row_label: Prose segment: PP-InsP5 Km

table_label: PubMed PMID 9822604 abstract

enzyme: Diphosphoinositol polyphosphate phosphohydrolase 1


enzyme_display_name: exopolyphosphatase

organism: Leishmania major

substrate_name: guanosine 5'-tetraphosphate

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: does not hydrolyze pyrophosphate, ATP, or p-nitrophenylphosphate

enzyme: exopolyphosphatase

substrate: guanosine 5'-tetraphosphate


enzyme_display_name: ADP-ribose pyrophosphatase

substrate_name: ADP-ribose

enzyme: ADP-ribose pyrophosphatase

substrate: ADP-ribose


organism: Enterobacter cloacae

proof_lines:
Enterobacter cloacae
ACC deaminase activity
lineweaver Burk plot


enzyme_display_name: ADP-ribose diphosphatase

organism: Methanocaldococcus jannaschii

substrate_name: ADPribose 2'-phosphate

enzyme: ADP-ribose diphosphatase

substrate: ADPribose 2'-phosphate


organism: Autographa californica multiple nucleopolyhedrovirus

assay_conditions_summary: pH 8; cofactor ADP


substrate_name: ADPribose

substrate: ADPribose


organism: Saccharomyces cerevisiae


organism: Synechococcus sp.

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

assay_conditions_summary: pH 9.5; cofactor ADP

column_label: PMID 15158734 DOI 10.1016/j.bbapap.2004.03.004 Table 1; row NuhA; columns Kcat (s^-1), Km (mM), and Kcat/Km (M^-1 s^-1).

row_label: NuhA / ADP-ribose

table_label: Table 1. Kinetic parameters of the recombinant NuhA and NuhA-DPfam for ADP-ribose


enzyme_display_name: diadenosine hexaphosphate hydrolase (AMP-forming)

organism: Arabidopsis thaliana


enzyme_display_name: Genome polyprotein

organism: Tick-borne encephalitis virus European subtype (strain Neudoerfl)

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: Genome polyprotein

substrate: ATP


enzyme: diadenosine hexaphosphate hydrolase (AMP-forming)


enzyme: Diphosphoinositol polyphosphate phosphohydrolase DDP1


enzyme_display_name: Diphosphoinositol polyphosphate phosphohydrolase 2

column_label: JBC Table II, row hDIPP2alpha, column K m (nM), for PP-InsP5 substrate reports 4.2 +/- 0.4.

raw_value_unit_evidence: Km raw_value=4.2 +/- 0.4 raw_unit=nM

table_label: Table II. Comparison of the catalytic properties of hDIPP isoforms with PP-InsP5 as substrate


column_label: Table I row Ap6A, column Km, reports 5.9 +/- 3.0 microM.

raw_value_unit_evidence: Ap6A Km=5.9 +/- 3.0 microM in Table I.

row_label: DIPP / Ap6A

table_label: JBC full text Table I


enzyme_display_name: inosine diphosphate phosphatase

substrate_name: ADP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

enzyme: inosine diphosphate phosphatase

substrate: ADP


enzyme_display_name: Ectonucleotide pyrophosphatase/phosphodiesterase family member 3

organism: Mus musculus

column_label: Article results prose states purified recombinant mENPP3 hydrolyzes cGAMP with KM = 76.5 +/- 18.7 uM at pH 9.0 in Figure 2C.

row_label: purified recombinant mouse ENPP3 hydrolyzing cGAMP

table_label: Results prose, Figure 2C


organism: Metapseudomonas resinovorans

assay_conditions_summary: pH 7.5; buffer 50 mM sodium phosphate

raw_value_unit_evidence: Table 1 row CarCCA10 / 6-Phenyl HODA columns: Km 2.51 uM; kcat 2.14 s^-1; kcat/Km 8.5 x 10^5 M^-1 s^-1.

row_label: CarCCA10 / 6-Phenyl HODA

table_label: Table 1. Kinetic parameters of native CarCCA10, ht-CarCCA10, and ht-CarCJ3


enzyme_display_name: diadenosine hexaphosphate hydrolase (ATP-forming)

organism: Thermus thermophilus

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

column_label: Table I. Kinetic constants for Ndx1; row Ap6A / ATP; columns kcat, Km, same-row quotient.

raw_value_unit_evidence: Table I Ap6A / ATP row: kcat 4.1 s^-1; Km 1.4 uM; printed kcat/Km 2.9 x 10^6 M^-1 s^-1.

row_label: Ap6A / ATP

table_label: Table I. Kinetic constants for Ndx1


organism: Burkholderia xenovorans LB400

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S112C to reconstruct the assayed variant sequence.


organism: Janthinobacterium sp. J3

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

column_label: Table 2; row ht-CarCJ3 / 6-Phenyl HODA; columns Km, kcat, same-row quotient.

raw_value_unit_evidence: Table 2 ht-CarCJ3 / 6-Phenyl HODA row: Km 2.73 uM; kcat 1.99 s^-1; printed scaled kcat/Km 7.3.

row_label: ht-CarCJ3 / 6-Phenyl HODA


organism: Paraburkholderia xenovorans

substrate_name: 4-nitrophenyl benzoate

substrate: 4-nitrophenyl benzoate


organism: Burkholderia xenovorans


organism: Paraburkholderia xenovorans (strain LB400)

substrate_name: HOPDA

substrate: HOPDA


enzyme_display_name: atrazine chlorohydrolase

organism: Pseudomonas sp.

substrate_name: hydroxyatrazine

enzyme: atrazine chlorohydrolase

substrate: hydroxyatrazine


enzyme_display_name: UniProt P9WNH5

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WNH5


enzyme_display_name: nucleoside-triphosphate phosphatase

organism: Southampton virus

enzyme: nucleoside-triphosphate phosphatase


substrate_name: Monochloroacetate

substrate: Monochloroacetate


substrate_name: Atrazine

column_label: Primary measurement evidence: evidence location type: table note; evidence location label: article page 1108 unnumbered kinetic-parameter table; measurement identity label: wild-type AtzA-AD1; atrazine; metric detail label: Km, kcat, and kcat/Km columns; assay condition: 100 mM Tris-HCl pH 7.2; atrazine 4.6-140 uM; 25 C; 10 min; HPLC; captured primary segment: wild-type AtzA-AD1 values were Km 146 +/- 10 uM, kcat 1.6 +/- 0.1 s^-1, and kcat/Km 1.1x10^4 +/- 0.1x10^4 s^-1 M^-1.

raw_value_unit_evidence: Page 1108 table note reports wild-type AtzA-AD1 Km 146 +/- 10 uM, kcat 1.6 +/- 0.1 s^-1, and kcat/Km 1.1x10^4 +/- 0.1x10^4 s^-1 M^-1.

row_label: Wild-type AtzA-AD1 values in table note

substrate: Atrazine


organism: uncultured archaeon

proof_lines: coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase


enzyme_display_name: 4-chlorobenzoyl-CoA dehalogenase

assay_conditions_summary: pH 7

enzyme: 4-chlorobenzoyl-CoA dehalogenase


organism: Escherichia coli


organism: Homo sapiens

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


substrate_name: CDP-choline

substrate: CDP-choline


substrate_name: cADP-ribose

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

substrate: cADP-ribose


organism: Pseudomonas fluorescens

proof_lines:
mutant A129/V227I
mutant V227I


proof_lines:
mutant A129/I199V
mutant I199V


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


enzyme_display_name: phosphonoacetaldehyde hydrolase

organism: Achromobacter insolitus

substrate_name: phosphonoacetaldehyde

enzyme: phosphonoacetaldehyde hydrolase

substrate: phosphonoacetaldehyde


enzyme_display_name: UniProt O31156

organism: Bacillus cereus

enzyme: UniProt O31156


enzyme_display_name: Phosphonoacetaldehyde hydrolase

organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: phosphonoacetaldehyde (at pH 7.0, 25 degrees Celsius)

enzyme: Phosphonoacetaldehyde hydrolase


organism: Spinacia oleracea

substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: sulfite

substrate: sulfite


organism: Archaeoglobus fulgidus


enzyme_display_name: haloalkane dehalogenase

organism: Sphingobium sp.

substrate_name: beta-hexachlorocyclohexane

enzyme: haloalkane dehalogenase

substrate: beta-hexachlorocyclohexane


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


substrate_name: ADP-D-ribose

assay_conditions_summary: pH 7; 310.15 K; cofactor ADP

substrate: ADP-D-ribose


proof_lines: mutant enzyme W28A/W46A, at pH 7.0 and 37°C


substrate_name: ADP-ribose

proof_lines:
pH 7.0, 37°C, wild-type enzyme
wild type enzyme, at pH 7.0 and 37°C
wild-type, pH 7.5, 37°C

substrate: ADP-ribose


enzyme_display_name: adenosylhomocysteinase

organism: Cytophaga hutchinsonii

substrate_name: S-adenosyl-L-homocysteine

proof_lines:
pH 7.5, 22°C
at pH 7.5 and 22°C

enzyme: adenosylhomocysteinase

substrate: S-adenosyl-L-homocysteine


enzyme_display_name: UniProt P10760

organism: Rattus norvegicus

substrate_name: S-adenosyl-DL-homocysteine

enzyme: UniProt P10760

substrate: S-adenosyl-DL-homocysteine


enzyme_display_name: UniProt P23526

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.2
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=41°C, pH=6.5

enzyme: UniProt P23526


enzyme_display_name: UniProt P74008

organism: Synechocystis sp. PCC 6803

enzyme: UniProt P74008


enzyme_display_name: UniProt Q9I685

organism: Pseudomonas aeruginosa

enzyme: UniProt Q9I685


organism: Pyrococcus horikoshii

proof_lines:
at pH 8.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=8.5


enzyme_display_name: ADP-ribose diphosphatase

organism: Bacillus methanolicus

substrate_name: ADPribose

assay_conditions_summary: pH 9.5; 323.15 K; cofactor ADP

enzyme: ADP-ribose diphosphatase

substrate: ADPribose


organism: Arthrobacter sp.


smiles: CCCCCCl


smiles: CCCCCl


smiles: CCCI


smiles: CC(C)CBr


smiles: CCI


organism: Bradyrhizobium japonicum


substrate_name: chlorocyclohexane

substrate: chlorocyclohexane


substrate_name: bromocyclohexane

substrate: bromocyclohexane


smiles: CC(CBr)Br


smiles: CCCCCCCl


smiles: CC(=C)CCl


organism: Classical swine fever virus

substrate_name: dUTP

mutation_signature: recombinant truncated protein ntNS3 / recombinant truncated protein ntNS3

mutation_type: truncation

proof_lines: pH 6.5, 37°C, recombinant truncated protein ntNS3, in absence of poly(U)

proof_lines: pH 6.5, 37°C, recombinant truncated protein ntNS3, in presence of poly(U)

substrate: dUTP


substrate_name: UTP

substrate: UTP


substrate_name: dCTP

substrate: dCTP


substrate_name: dGTP

substrate: dGTP


substrate_name: ATP

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: dATP

substrate: dATP


substrate_name: CTP

substrate: CTP


substrate_name: GTP

substrate: GTP


enzyme_display_name: exopolyphosphatase

organism: Escherichia coli

substrate_name: (Polyphosphate)n

smiles: N#N

enzyme: exopolyphosphatase

substrate: (Polyphosphate)n


substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens

substrate_name: XDP

substrate: XDP


substrate_name: ITP

substrate: ITP


substrate_name: ADP

substrate: ADP


proof_lines: with ADP as substrate, at pH 7.5 and 37°C

proof_lines: with ITP as substrate, at pH 7.5 and 37°C

proof_lines: with IDP as substrate, at pH 7.5 and 37°C


proof_lines: pH 8.0, 25°C, mutant enzyme D235A, approximate value from activity of the cell extract


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


enzyme_display_name: nucleotide diphosphatase

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

enzyme: nucleotide diphosphatase


substrate_name: cAMP

substrate: cAMP


assay_conditions_summary: pH 7.4; 297.15 K; cofactor ATP

proof_lines: versus 4-nitrophenyl 5'-thymidine monophosphate, pH 9.0, 37°C, NPP1


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: E-NPP1, in 10 mM HEPES, 1 mM MgCl2, and 2 mM CaCl2, pH 7.4, at 37°C

proof_lines: E-NPP3, in 10 mM HEPES, 1 mM MgCl2, and 2 mM CaCl2, pH 7.4, at 37°C


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


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Hepacivirus hominis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, NTP hydrolysis-dependent helicase activity

proof_lines: pH 7.5, 25°C, inhibition of ATPase activity


substrate_name: 2',3'-didehydro-thymidine triphosphate

substrate: 2',3'-didehydro-thymidine triphosphate


substrate_name: ddTTP

substrate: ddTTP


substrate_name: dTTP

substrate: dTTP


substrate_name: ddCTP

substrate: ddCTP


substrate_name: dCTP

substrate: dCTP


organism: Staphylococcus aureus

proof_lines: mutant E126A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

substrate: ATP


proof_lines: mutant Y88A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


proof_lines: N45A, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, presence of 10 mM Mn2+, pH 7.5, temperature not specified in the publication


organism: Agrobacterium tumefaciens

smiles: C(CCl)CCl

proof_lines: below, recombinant wild-type enzyme, pH 8.6, 37°C

proof_lines: above, recombinant wild-type enzyme and mutant Y109W, pH 8.6, 37°C


proof_lines: recombinant wild-type enzyme, pH 8.6, 37°C


smiles: C(CI)CI


smiles: CCCCCCBr


enzyme_display_name: GTP cyclohydrolase II

organism: Bacillus subtilis

enzyme: GTP cyclohydrolase II


proof_lines: mutant enzyme Y210C/A290T/Q293R/A296T/K322R/M361I, at pH 8.5 and 30°C


proof_lines: mutant enzyme Y210C/A290T/Q293R/A296T/K322R/F339Y/M361I, at pH 8.5 and 30°C


organism: Bos taurus


substrate_name: UTP

substrate: UTP


substrate_name: CTP

substrate: CTP


substrate_name: CDP

substrate: CDP


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: 3-Aminopyridine adenine dinucleotide

substrate: 3-Aminopyridine adenine dinucleotide


substrate_name: adenosine diphosphoribose

substrate: adenosine diphosphoribose


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 8-oxo-dGDP phosphatase

assay_conditions_summary: pH 8; 303.15 K; buffer Tris-HCl; cofactor ADP

proof_lines:
pH 8.0, 30°C
in Tris-HCl buffer (pH 8.0), at 37°C

enzyme: 8-oxo-dGDP phosphatase


assay_conditions_summary: pH 8; 303.15 K; cofactor ADP


substrate_name: dADP

substrate: dADP


substrate_name: dGDP

substrate: dGDP


organism: Caulobacter vibrioides

proof_lines:
pH 8.2, 25°C
at pH 8.2 and 25°C


smiles: C(CCCl)CCCl