substrate_name: Carbamoyl phosphate

smiles: NC(=O)OP(=O)(O)O

column_label: Table 2 (Kinetic Parameters for the ATP Synthesis Reaction), enzyme row 'C230A'; column 'k_cat (min^-1)' = 0.42; column 'K_m ADP (mM)' = 0.62; column 'K_m CbmP (mM)' = 7.94. This catalog row reads the k_cat column and the K_m CbmP (mM) column. Table 2 has only these three value columns and carries no catalytic-efficiency column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.42 min-1; one min^-1 is one sixtieth of a s^-1, so 0.42 / 60 = 0.007 s^(-1), which is the paper value in catalog units. Km: printed Table 2 cell 7.94 mM; already in mM, so no unit conversion applies (this paper prints no uM kinetic cell); the paper value is 7.94 mM. kcat/Km: Table 2 has no catalytic-efficiency column, so the paper value 0.0008816120906801007 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.007 / 7.94 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2 (Kinetic Parameters for the ATP Synthesis Reaction), enzyme row 'C230A': the k_cat (min^-1) cell reads 0.42 min-1 and the K_m CbmP (mM) cell reads 7.94 mM. Table 2 carries no catalytic-efficiency column, so it prints no kcat/Km cell for this row.

substrate: Carbamoyl phosphate


enzyme_display_name: biotin carboxylase

organism: Escherichia coli

source_db: oed

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K238Q to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

data_origin: experimental

enzyme: biotin carboxylase

source: oed


mutation_signature: Unknown

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


substrate_name: hydrogencarbonate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C230A to reconstruct the assayed variant sequence.

substrate: hydrogencarbonate


enzyme_display_name: carbamoyl-phosphate synthase (ammonia)

organism: Homo sapiens

substrate_name: NH3; CO2; ATP; H2O

kcat_display: Not reported

kcat_over_km_display: Not reported

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

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T344A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: carbamoyl-phosphate synthase (ammonia)(Enzyme) mutant p.Thr344Ala

enzyme: carbamoyl-phosphate synthase (ammonia)

substrate: NH3; CO2; ATP; H2O


substrate_name: CO2; H2O; NH3; ATP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N355D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbamoyl-phosphate synthase (ammonia)(Enzyme) mutant p.Asn355Asp

substrate: CO2; H2O; NH3; ATP


substrate_name: CO2; NH3; H2O; ATP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T544M with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbamoyl-phosphate synthase (ammonia)(Enzyme) mutant p.Thr544Met

substrate: CO2; NH3; H2O; ATP


substrate_name: ATP; CO2; H2O; NH3

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A1378T to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbamoyl-phosphate synthase (ammonia)(Enzyme) mutant p.Ala1378Thr

substrate: ATP; CO2; H2O; NH3


substrate_name: CO2; NH3; ATP; H2O

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G1376S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbamoyl-phosphate synthase (ammonia)(Enzyme) mutant p.Gly1376Ser

substrate: CO2; NH3; ATP; H2O


substrate_name: NH3; H2O; ATP; CO2

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T1443A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: carbamoyl-phosphate synthase (ammonia)(Enzyme) mutant p.Thr1443Ala

substrate: NH3; H2O; ATP; CO2


enzyme_display_name: biotin--[biotin carboxyl-carrier protein] ligase

organism: Staphylococcus aureus

substrate_name: biotin

source_db: brenda

substrate: biotin

source: brenda


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: Ki above 0.01 mM, wild type enzyme, at pH 7.5 and 37°C

enzyme: biotin--[biotin carboxyl-carrier protein] ligase

substrate: Unknown


substrate_name: ATP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: biotin acetylene

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F123R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F123R, pH and temperature not specified in the publication

substrate: biotin acetylene


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F123G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F123G, pH and temperature not specified in the publication


organism: Aquarana catesbeiana

substrate_name: ammonia

smiles: N

proof_lines: wild-type enzyme, comparison to native and mutant enzyme

substrate: ammonia


organism: Mycobacterium tuberculosis

source_db: skid

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

sequence_source: multiple

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: kcat is 0.034 sec(-1) with biotin as substrate. kcat is 0.0282 sec(-1) with Mg/ATP as substrate. kcat is 0.030 sec(-1) with apo-BCCP as substrate (PubMed:18509457). kcat is 0.017 sec(-1) with ATP as substrate (PubMed:24723382).

source_databases_merged: skid uniprot

source: skid


enzyme_display_name: phosphoribosylamine--glycine ligase

organism: Cryptococcus neoformans (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)

substrate_name: ATP (at 37 degrees Celsius)

source_db: uniprot

proof_lines: kcat is 27.3 sec(-1) for phosphoribosylamine--glycine ligase activity (at 37 degrees Celsius).

enzyme: phosphoribosylamine--glycine ligase

substrate: ATP (at 37 degrees Celsius)

source: uniprot


substrate_name: glycine (at 37 degrees Celsius)

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

substrate: glycine (at 37 degrees Celsius)


organism: Rattus norvegicus

proof_lines: The activation constant Ka of N-acetyl-L-glutamate for the reaction is 0.11 mM.


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP


smiles: O=C=O

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ADP


substrate_name: N-Carbamyl-L-glutamate

substrate: N-Carbamyl-L-glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R16E to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

verification_status: verified

column_label: Primary-paper Wiley article/ePDF prose reports apparent Km values for D-biotin, ATP, and apo-MCCase as 130 nM, 4.4 uM, and 32 uM respectively.

raw_value_unit_evidence: D-biotin apparent Km 130 nM

row_label: D-biotin substrate in apparent Km sentence

table_label: Primary-paper abstract/prose kinetic statement

status: verified


raw_value_unit_evidence: ATP apparent Km 4.4 uM

row_label: ATP substrate in apparent Km sentence


organism: Methanobrevibacter smithii

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


verification_status: unverified

status: unverified


organism: Escherichia coli (strain K12)


substrate_name: glycine

substrate: glycine


substrate_name: ADP

substrate: ADP


proof_lines: recombinant biotin carboxylase was enzymatically active in carboxylating free biotin


substrate_name: bicarbonate

substrate: bicarbonate


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

proof_lines: Carbamyl phosphate formation by the enzyme is shown to be dependent upon ATP, ammonia, bicarbonate, and magnesium ions.


substrate_name: hydrogencarbonate

substrate: hydrogencarbonate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


proof_lines: kcat is 0.228 sec(-1) with ATP as substrate (at pH 8) (PubMed:16793549). kcat is 0.44 sec(-1) with hydrogencarbonate as substrate (at pH 8) (PubMed:19213731). kcat is 0.58 sec(-1) with biotin as substrate (at pH 8) (PubMed:19213731).


organism: Zymoseptoria tritici

assay_conditions_summary: pH 8


enzyme_display_name: glutamate--methylamine ligase

organism: Methylovorus mays

substrate_name: methylamine

smiles: CN

column_label: Table 4; row label: Methylamine; column labels: Relative activity (%) and Km (mM); raw values 100% and 0.18 mM; normalized Km 0.18 mM.

normalized_value_unit_evidence: Km=0.18 mM as reported in Table 4.

raw_value_unit_evidence: Table 4; substrate methylamine; relative activity 100%; Km = 0.18 mM.

row_label: Substrate row: Methylamine; column: Km (mM); relative activity column also present; UniProt A9ZPH9 EC 6.3.4.12 (glutamate--methylamine ligase) linked to PMID 17284842.

table_label: Table 4. Reactivity of Theanine-Forming Enzyme to Various Amines and Km Values for Substrates

enzyme: glutamate--methylamine ligase

substrate: methylamine


substrate_name: ethylamine

smiles: CCN

column_label: Table 4; row label: Ethylamine; column labels: Relative activity (%) and Km (mM); raw values 75% and 0.57 mM; normalized Km 0.57 mM.

normalized_value_unit_evidence: Km=0.57 mM as reported in Table 4.

raw_value_unit_evidence: Table 4; substrate ethylamine; relative activity 75%; Km = 0.57 mM.

row_label: Substrate row: Ethylamine; column: Km (mM); relative activity column also present; UniProt A9ZPH9 EC 6.3.4.12 (glutamate--methylamine ligase) linked to PMID 17284842.

substrate: ethylamine


substrate_name: hydroxylamine

smiles: NO

column_label: Table 4; row label: Hydroxylamine; column labels: Relative activity (%) and Km (mM); raw values 40% and 3.9 mM; normalized Km 3.9 mM.

normalized_value_unit_evidence: Km=3.9 mM as reported in Table 4.

raw_value_unit_evidence: Table 4; substrate hydroxylamine; relative activity 40%; Km = 3.9 mM.

row_label: Substrate row: Hydroxylamine; column: Km (mM); relative activity column also present; UniProt A9ZPH9 EC 6.3.4.12 (glutamate--methylamine ligase) linked to PMID 17284842.

substrate: hydroxylamine


column_label: Table 4; row label: Ammonia; column labels: Relative activity (%) and Km (mM); raw values 0.75% and 84 mM; normalized Km 84.0 mM.

normalized_value_unit_evidence: Km=84.0 mM as reported in Table 4.

raw_value_unit_evidence: Table 4; substrate ammonia; relative activity 0.75%; Km = 84 mM.

row_label: Substrate row: Ammonia; column: Km (mM); relative activity column also present; UniProt A9ZPH9 EC 6.3.4.12 (glutamate--methylamine ligase) linked to PMID 17284842.


substrate_name: glutamic acid (with methylamine as substrate)

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

proof_lines: Table 4: Reactivity of Theanine-Forming Enzyme to Various Amines and Km Values for Substrates

proof_lines: glutamic-acid context with methylamine and ethylamine


substrate_name: ATP (with methylamine as substrate)

proof_lines: ATP context with methylamine and ethylamine

substrate: ATP (with methylamine as substrate)


substrate_name: dihydroorotate

substrate: dihydroorotate


substrate_name: N-carbamoyl-L-aspartate

substrate: N-carbamoyl-L-aspartate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: glutamine

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

column_label: PubMed abstract says the Km values for glutamine and bicarbonate are 5 X 10(-4) M and 3 X 10(-3) M, respectively; glutamine maps to 5 X 10(-4) M.

raw_value_unit_evidence: Km raw_value=5 X 10(-4) raw_unit=M

row_label: CPSase activity; substrate glutamine

table_label: PMID 182284 PubMed abstract

substrate: glutamine


column_label: PubMed abstract says the Km values for glutamine and bicarbonate are 5 X 10(-4) M and 3 X 10(-3) M, respectively; bicarbonate maps to 3 X 10(-3) M.

raw_value_unit_evidence: Km raw_value=3 X 10(-3) raw_unit=M

row_label: CPSase activity; substrate bicarbonate


substrate_name: aspartate

substrate: aspartate


substrate_name: carbamoyl phosphate

substrate: carbamoyl phosphate


substrate_name: bilirubin-glucuronoside

column_label: Article abstract kinetic prose / rat MRP2 / MGB: Km 0.8 micromol/L; normalized Km 0.0008 mM.

raw_value_unit_evidence: K(m) values were 0.7 and 0.9 micromol/L for human MRP2, and 0.8 and 0.5 micromol/L for rat MRP2, with MGB and BGB as substrates, respectively. Matched row: rat MRP2 / MGB; raw Km 0.8 micromol/L.

row_label: rat MRP2 / MGB

table_label: Article abstract / recombinant human and rat MRP2 Km values for bilirubin conjugates

substrate: bilirubin-glucuronoside


substrate_name: bilirubin-bisglucuronoside

column_label: Article abstract kinetic prose / rat MRP2 / BGB: Km 0.5 micromol/L; normalized Km 0.0005 mM.

raw_value_unit_evidence: K(m) values were 0.7 and 0.9 micromol/L for human MRP2, and 0.8 and 0.5 micromol/L for rat MRP2, with MGB and BGB as substrates, respectively. Matched row: rat MRP2 / BGB; raw Km 0.5 micromol/L.

row_label: rat MRP2 / BGB

substrate: bilirubin-bisglucuronoside


enzyme_display_name: ABC-type xenobiotic transporter

substrate_name: urate

column_label: Abstract and Table 1, row [14C]urate, Km column = 1,550 +/- 270 uM; abstract reports 1.5 +/- 0.3 mM

normalized_value_unit_evidence: 1.5 mM (table normalized 1.55 mM)

table_label: Table 1

enzyme: ABC-type xenobiotic transporter

substrate: urate


substrate_name: cGMP

column_label: Abstract and Table 1, row [3H]cGMP, Km column = 180 +/- 20 uM; abstract reports 180 +/- 20 uM

normalized_value_unit_evidence: 0.18 mM (table normalized 0.18 mM)

substrate: cGMP


substrate_name: biotin

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

substrate: biotin


substrate_name: malonyl-CoA

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

assay_conditions_summary: cofactor CoA

substrate: malonyl-CoA


substrate_name: leukotriene C4

substrate: leukotriene C4


substrate_name: ATP

substrate: ATP


column_label: The abstract reports the enzyme had unusually high affinity for ATP (Km = 0.2 mM).

raw_value_unit_evidence: Km raw_value=0.2 mM raw_unit=mM

row_label: Prose segment: ATP Km

table_label: PubMed PMID 206652 abstract


enzyme_display_name: ABC-type heme transporter

substrate_name: ATP (from purified mitochondrial ABCB6)

enzyme: ABC-type heme transporter

substrate: ATP (from purified mitochondrial ABCB6)


substrate_name: coproporphyrin III (from liposome-reconstituted purified mitochondrial ABCB6)


enzyme_display_name: ABC-type D-galactose transporter

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

column_label: Abstract states the MglA ATPase has Km ATP = 60 microM.

raw_value_unit_evidence: Km raw_value=60 raw_unit=microM

row_label: Salmonella typhimurium MglA galactose-stimulated ATPase with ATP

table_label: PubMed abstract PMID 8387496

enzyme: ABC-type D-galactose transporter


enzyme_display_name: P-type phospholipid transporter

organism: Bos taurus

substrate_name: ATP (with a purified ABCA4)

enzyme: P-type phospholipid transporter

substrate: ATP (with a purified ABCA4)


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature A1378T to reconstruct the assayed variant sequence.

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=7.4


enzyme_display_name: ABC-type lipid A-core oligosaccharide transporter


assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table 2 lists the ATP Km (uM) row and ATP11B column as 730 +/- 190.

raw_value_unit_evidence: Km raw_value=730 +/- 190 raw_unit=uM.

row_label: ATP Km (uM)

table_label: Table 2 Kinetic Parameters for ATP11-CDC50A Complexes


enzyme_display_name: ABC-type D-ribose transporter

enzyme: ABC-type D-ribose transporter


enzyme_display_name: ABC-type polyamine transporter

enzyme: ABC-type polyamine transporter


enzyme_display_name: ABC-type putrescine transporter

substrate_name: putrescine

smiles: C(CCN)CN

enzyme: ABC-type putrescine transporter

substrate: putrescine


organism: Mus musculus

column_label: Table 2 lists the ATP Km (uM) row and ATP11C column as 1440 +/- 110.

raw_value_unit_evidence: Km raw_value=1440 +/- 110 raw_unit=uM.


organism: Homo sapiens

column_label: Science full text Fig. 1C caption/prose maps ATP8A1-CDC50a, POPS, and Km 111.0 +/- 26.4 uM directly to the target row.

raw_value_unit_evidence: Fig. 1C caption/prose reports Km=111.0 +/- 26.4 uM for 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-l-serine (POPS).

row_label: ATP8A1-CDC50a in GDN micelles with POPS

table_label: Science full text Fig. 1C caption/prose: Phospholipid-dependent ATPase activity of ATP8A1


column_label: PMC3525726 results prose states that the ABCC10 K_m value for ATP binding is 3.2 mM.

raw_value_unit_evidence: Results prose reports ABCC10 K_m for ATP binding raw_value=3.2 raw_unit=mM.

row_label: Human ABCC10 ATP binding

table_label: PMC3525726 ATPase kinetics results prose


substrate_name: methotrexate

substrate: methotrexate


substrate_name: GSSG (at pH 8)

substrate: GSSG (at pH 8)


substrate_name: N-[(S)-lactoyl]-L-phenylalanine

substrate: N-[(S)-lactoyl]-L-phenylalanine


substrate_name: ATP (at 28 degrees Celsius)

substrate: ATP (at 28 degrees Celsius)


verification_status: corrected

column_label: The official PubMed abstract reports: MRP4 hydrolyzes ATP (Km, 0.62 mm).

raw_value_unit_evidence: Km raw_value=0.62 mm raw_unit=mm

row_label: Prose segment: MRP4 hydrolyzes ATP

table_label: PubMed PMID 15364914 abstract

status: corrected


substrate_name: 17beta-estradiol 17-glucosiduronic acid

substrate: 17beta-estradiol 17-glucosiduronic acid


substrate_name: indoxyl sulfate

column_label: Full text reports ABCG2 mediates ATP-dependent transport of indoxyl sulfate with a Km of 25.3 mM and Vmax of 5.27 nmol/min/mg protein in Figure 3b.

raw_value_unit_evidence: Km raw_value=25.3 mM raw_unit=mM

row_label: ABCG2 vesicle transport of indoxyl sulfate

table_label: PMC full text Figure 3b kinetic prose PMID 30042379

substrate: indoxyl sulfate


substrate_name: taurolithocholate sulfate

column_label: PubMed abstract states that the mean K(m) value for uptake of [(3)H]TLC-S by hBSEP was 9.5+/-1.5 microM, a value similar to that for hMRP2 (8.2+/-1.3 microM).

raw_value_unit_evidence: Km raw_value=8.2+/-1.3 raw_unit=microM

row_label: human MRP2/ABCC2 with taurolithocholate 3-sulfate (TLC-S)

table_label: PubMed abstract PMID 16332456

substrate: taurolithocholate sulfate


organism: Oryctolagus cuniculus


substrate_name: taurolithocholate 3-sulfate

substrate: taurolithocholate 3-sulfate


organism: Plasmodium falciparum (isolate 3D7)

column_label: PMC Results state fitting ATP hydrolytic activity to Michaelis-Menten kinetics gives Vmax 198.3 +/- 7.6 nmol min-1 mg-1 and Km 0.33 +/- 0.04 mM ATP; Fig. 1A caption repeats wild-type PfMDR1 has Km 0.33 +/- 0.04 mM.

raw_value_unit_evidence: Km raw_value=0.33 +/- 0.04 raw_unit=mM

row_label: wild-type Plasmodium falciparum PfMDR1 ATPase activity with ATP

table_label: PMC full-text PMID 37527341 / Fig. 1A and Results paragraph


assay_conditions_summary: 300.15 K; cofactor ATP

column_label: Abstract reports ATP-dependent transport of DHEAS by MRP4 showed saturable kinetics with Km and Vmax values of 2 microM and 45 pmol/mg per min, respectively, at 27 degrees C.

raw_value_unit_evidence: Km raw_value=2 microM raw_unit=microM

row_label: Human MRP4 / dehydroepiandrosterone 3-sulfate (DHEAS)

table_label: PubMed XML abstract PMID 12523936


column_label: The abstract reports Vmax and Km values of approximately 0.8 s^-1 and 50+/-8 microM for basal Yor1p ATPase activity.

raw_value_unit_evidence: Km raw_value=50+/-8 microM raw_unit=microM

table_label: PubMed PMID 17950691 abstract


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

proof_lines: mutant I364A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant I364A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant I364S, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant I364S, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant I364Q, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant I364Q, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant T369A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant N360A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant I362A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant I362A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant F88A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant F88A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant Y358A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C


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

proof_lines: wild-type, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: wild-type, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant F354A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant L112A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant L112A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant K374A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant L361A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant I115A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant I115A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant S365A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant S365A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant I364E, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant I364E, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant I364M, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant I364M, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant I364F, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant I364F, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


proof_lines: mutant N359A, presence of phosphatidylserine, K0.5 value, pH 7.5, 37°C

proof_lines: mutant N359A, presence of phosphatidylethanolamine, K0.5 value, pH 7.5, 37°C


enzyme_display_name: ABC-type vitamin B12 transporter

substrate_name: cobalamin

assay_conditions_summary: 310.15 K; cofactor ATP

column_label: Results state that Lineweaver-Burk analysis gave Km and Vmax values of 426 microM and 667 pmol/min/mg, respectively.

raw_value_unit_evidence: Km raw_value=426 microM raw_unit=microM

row_label: human ABCD4 liposomes loaded with cobalamin

table_label: PMC full-text PMID 33845046 / Figure S5 kinetics described in Results

enzyme: ABC-type vitamin B12 transporter

substrate: cobalamin


substrate_name: coproporphyrin III

column_label: Results report wild-type ATP-dependent CP transport with Vmax 9.8 pmol min^-1 mg^-1 and Km 12.6 uM.

raw_value_unit_evidence: Km raw_value=12.6 raw_unit=uM

row_label: wild-type ATP-dependent CP transport

table_label: PMC3339991 Figure 2B / Results prose

substrate: coproporphyrin III


column_label: Abstract reports ATP-dependent uptake of tritiated TLC-S (Km=3.9 microM) in Mrp2-expressing Sf9 membrane vesicles.

raw_value_unit_evidence: Km raw_value=3.9 microM raw_unit=microM

row_label: Rat Mrp2-expressing Sf9 membrane vesicles / taurolithocholate sulfate (TLC-S)

table_label: PubMed XML abstract PMID 11248200


organism: Escherichia coli

substrate_name: ADP

proof_lines: pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with carbamoyl phosphate as cosubstrate

substrate: ADP


assay_conditions_summary: pH 8; 298.15 K; cofactor ADP

proof_lines: pH 8, 25°C, E211A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate


proof_lines: pH 8, 25°C, E288A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate


proof_lines: pH 8, 25°C, N290A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate


substrate_name: Carbamoyl phosphate

proof_lines: pH 8, 25°C, E211A mutant, ATP synthesis reaction with ADP as cosubstrate

substrate: Carbamoyl phosphate


proof_lines: pH 8, 25°C, R292A mutant, ATP synthesis reaction with carbamoyl phosphate as cosubstrate


proof_lines: pH 8, 25°C, E288A mutant, ATP synthesis reaction with ADP as cosubstrate


proof_lines: pH 8, 25°C, R292A mutant, ATP synthesis reaction with ADP as cosubstrate


substrate_name: biotin

substrate: biotin


proof_lines: mutant R317E, E147Kmutant BCCP biotin domain


substrate_name: ATP

substrate: ATP


proof_lines: mutant R317E, wild-type BCCP biotin domain

proof_lines: wild-type enzyme, E147Kmutant BCCP biotin domain

proof_lines: mutant K277E, wild-type BCCP biotin domain


proof_lines: mutant K283E, E147Kmutant BCCP biotin domain


assay_conditions_summary: pH 8.3; 303.15 K; cofactor ATP

proof_lines:
wild-type enzyme
wild-type, pH 8.3, 30°C


proof_lines: mutant K277E, E147Kmutant BCCP biotin domain


proof_lines: mutant K321E, E147Kmutant BCCP biotin domain


substrate_name: N-acetylglutamate

substrate: N-acetylglutamate


proof_lines: recombinant wild type enzyme, in 50 mM glycyl-glycine pH 7.4, 70 mM KCl, 1 mM dithiothreitol, 20 mM MgSO4, at 37°C


organism: Plasmodium falciparum


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

enzyme: ABC-type lipid A-core oligosaccharide transporter


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: mutant enzyme Y389C, in 50 mM glycyl-glycine pH 7.4, 70 mM KCl, 1 mM dithiothreitol, 20 mM MgSO4, at 37°C


proof_lines: mutant enzyme T344A, in 50 mM glycyl-glycine pH 7.4, 70 mM KCl, 1 mM dithiothreitol, 20 mM MgSO4, at 37°C


proof_lines: mutant enzyme G1376S, in 50 mM glycyl-glycine pH 7.4, 70 mM KCl, 1 mM dithiothreitol, 20 mM MgSO4, at 37°C


proof_lines: mutant enzyme N355D, in 50 mM glycyl-glycine pH 7.4, 70 mM KCl, 1 mM dithiothreitol, 20 mM MgSO4, at 37°C


proof_lines: mutant enzyme T1443A, in 50 mM glycyl-glycine pH 7.4, 70 mM KCl, 1 mM dithiothreitol, 20 mM MgSO4, at 37°C


proof_lines: mutant enzyme T544M, in 50 mM glycyl-glycine pH 7.4, 70 mM KCl, 1 mM dithiothreitol, 20 mM MgSO4, at 37°C


proof_lines: ATPase activity of the mutant L76P potA subunit


proof_lines: ATPase activity of the mutant E297Q potA subunit


proof_lines: ATPase activity of the mutant E297K potA subunit


proof_lines: ATPase activity of the mutant E297D potA subunit


proof_lines: ATPase activity of the mutant F47L potA subunit


proof_lines: ATPase activity of the mutant L60F potA subunit


proof_lines: ATPase activity of the mutant F27L potA subunit


organism: Macaca fascicularis

substrate_name: leukotriene C4/in

substrate: leukotriene C4/in


substrate_name: Estrone 3-sulfate

substrate: Estrone 3-sulfate


substrate_name: probenecid

substrate: probenecid


substrate_name: methotrexate

substrate: methotrexate


proof_lines: 25°C, wild-type enzyme, bicarbonate-dependent ATP hydrolysis in the absence of biotin

proof_lines: biotin-dependent ATP hydrolysis, wild-type enzyme

proof_lines: wild type enzyme, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C


assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: 25°C, C230A mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin

proof_lines: 25°C, C230A mutant, biotin-dependent ATP hydrolysis


proof_lines: 25°C, K238Q mutant, bicarbonate-dependent ATP hydrolysis in the absence of biotin


proof_lines:
pH 7.4 wild-type
25°C, free biotin, wild-type enzyme
pH 8, 25°C, wild-type enzyme


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines: pH 8, 25°C, wild-type enzyme, ATP synthesis reaction with ADP as cosubstrate


proof_lines:
N290A mutant, homodimer
pH 8, 25°C, N290A mutant


proof_lines:
pH 8, 25°C, hybrid dimer K238Q/WT
K238Q mutant


proof_lines:
R292A mutant, homodimer
pH 8, 25°C, R292A mutant


organism: Gallus gallus


substrate_name: sarcosine

smiles: CNCC(=O)O

substrate: sarcosine


substrate_name: beta-Ala

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

substrate: beta-Ala


substrate_name: Gly

substrate: Gly


enzyme_display_name: ABC-type quaternary amine transporter

organism: Bacillus subtilis

proof_lines: wild-type, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form

enzyme: ABC-type quaternary amine transporter


proof_lines: mutant S45C, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form


proof_lines: mutant F19W, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form


proof_lines: mutant G161C, performed in 10 mM sodium phosphate, pH 7.5 and 1 M NaCl, monomeric form


assay_conditions_summary: cofactor ATP

proof_lines: biotin-dependent ATP hydrolysis, mutant enzyme E23R


proof_lines: biotin-dependent ATP hydrolysis, mutant enzyme R19E


proof_lines: biotin-dependent ATP hydrolysis, mutant enzyme F363A


assay_conditions_summary: cofactor ADP


substrate_name: phosphate

substrate: phosphate


substrate_name: desthiobiotin

substrate: desthiobiotin


organism: Methanobrevibacter smithii


organism: Cricetulus griseus

substrate_name: tetramethylrhodamine/in

proof_lines: pH 7.5, 37°C, sigmoidal inhibition plot, Hill coefficient n=1.77

substrate: tetramethylrhodamine/in


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: estradiol 17-beta-D-glucuronide/in

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F368W to reconstruct the assayed variant sequence.

substrate: estradiol 17-beta-D-glucuronide/in


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F368Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W995F to reconstruct the assayed variant sequence.


organism: Aquifex aeolicus

substrate_name: glycine

substrate: glycine


assay_conditions_summary: pH 7.9; 363.15 K; cofactor ATP


substrate_name: epsilon-ATP

substrate: epsilon-ATP


proof_lines:
Vmax, free biotin
free biotin


substrate_name: biotin-carboxyl-carrier protein

proof_lines: Vmax, C-terminal 87 amino acids of the biotinylated biotin-carboxyl-carrier protein

substrate: biotin-carboxyl-carrier protein


substrate_name: paclitaxel

proof_lines: pH 7.5, 37°C, presence of 5% cholesterol

proof_lines: pH 7.5, 37°C, presence of 20% cholesterol

substrate: paclitaxel


substrate_name: vincristine

substrate: vincristine


substrate_name: rhodamine B

substrate: rhodamine B


substrate_name: rhodamine 123

substrate: rhodamine 123


substrate_name: digoxin

substrate: digoxin


substrate_name: dexamethasone

substrate: dexamethasone


organism: Phycomyces blakesleeanus

substrate_name: ATP

substrate: ATP


substrate_name: biotin

substrate: biotin


substrate_name: lipid A

proof_lines: pH 7.5, 37°C, recombinant His-tagged enzyme

substrate: lipid A


substrate_name: lipopolysaccharide

substrate: lipopolysaccharide


organism: Geobacillus thermodenitrificans

proof_lines: recombinant biotin carboxylase domain of pyruvate carboxylase


proof_lines: mutant enzyme Q475A, in the absence of nicardipine, at 37°C, pH not specified in the publication

proof_lines: mutant enzyme Q475A, in the presence of 0.05 mM nicardipine, at 37°C, pH not specified in the publication


proof_lines: wild type enzyme, in the absence of nicardipine, at 37°C, pH not specified in the publication

proof_lines: wild type enzyme, in the presence of 0.05 mM nicardipine, at 37°C, pH not specified in the publication


substrate_name: ADP

substrate: ADP


organism: Klebsiella aerogenes


substrate_name: Gly

substrate: Gly


organism: Salmonella enterica subsp. enterica serovar Typhimurium


proof_lines: pH 7.4, 37°C, native enzyme, value for basal ATPase activity with no transport substrate

proof_lines: pH 7.4, 37°C, trypsin-cleaved enzyme, value for basal ATPase activity with no transport substrate

proof_lines: pH 7.4, 37°C, chymotrypsin-cleaved enzyme, value for basal ATPase activity with no transport substrate


substrate_name: digoxin/in

proof_lines: pH 7.4, 37°C, chymotrypsin-cleaved enzyme

substrate: digoxin/in


organism: Mycobacterium tuberculosis

substrate_name: d-biotin

substrate: d-biotin


assay_conditions_summary: pH 8; 310.15 K; cofactor ADP


organism: Streptococcus pneumoniae

substrate_name: GTP

substrate: GTP


organism: Drosophila melanogaster

substrate_name: leukotriene C4/in

substrate: leukotriene C4/in


substrate_name: glycine betaine

proof_lines:
OpuA
OpuC, without NaCl
OpuC, in presence of 0.4 M NaCl

substrate: glycine betaine


proof_lines: reconstituted purified recombinant His-tagged enzyme in liposomes prepared from Escherichia coli phospholipids, pH 7.5, 37°C, ATP hydrolysis in presence of 10 mM Mg2+ and 0.021 mM Kdo2-lipid A

proof_lines: in 50 mM HEPES (pH 7.5), 10 mM MgCl2, at 37°C


substrate_name: spermidine/out

proof_lines:
spermidine-preferential system
putrescine-specific system

substrate: spermidine/out


organism: Bos taurus

proof_lines: pH and temperature not specified in the publication


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

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: mutant enzyme R16E, in 100 mM HEPES (pH 8.0), 5 mM MgCl2, at 30°C


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

proof_lines: wild type enzyme, with 20 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C

proof_lines: wild type enzyme, with 1.5 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C

proof_lines: wild type enzyme, with 10 mM Mg-ATP, in 100 mM HEPES (pH 8.0), at 30°C


substrate_name: avitag-tagged maltose-binding protein

substrate: avitag-tagged maltose-binding protein


enzyme_display_name: ABC-type thiamine transporter

proof_lines: at 37°C, pH not specified in the publication

enzyme: ABC-type thiamine transporter


proof_lines:
pure subunit BtuD, pH 7.5, 37°C
BtuCD complex, pH 7.5, 37°C


organism: Helicoverpa armigera

assay_conditions_summary: pH 7.4; 295.15 K; cofactor ATP

proof_lines: 22°C, pH 7.4, activation by ethylparaoxon (0.03 mM) or fenvalerate (0.03 mM)


organism: Escherichia coli

assay_conditions_summary: cofactor CoA


proof_lines:
in presence of spermine
without spermine
ATPase activity of PotA


organism: Homo sapiens

substrate_name: verapamil

proof_lines: pH 7.4, 37°C, EPR spin-labeled verapamil

proof_lines: pH 7.5, 37°C, presence of 20% cholesterol

proof_lines: pH 7.5, 37°C, presence of 5% cholesterol

substrate: verapamil


substrate_name: quinidine

substrate: quinidine


organism: Saccharomyces cerevisiae


proof_lines: reaction with ATP + apo-carboxyl carrier protein, a subunit of acetyl-CoA carboxylase from E. coli


substrate_name: dimethylarsenic acid[side 1]

proof_lines: wild type enzyme, at 37°C, pH not specified in the publication

substrate: dimethylarsenic acid[side 1]


organism: Lactococcus lactis

substrate_name: betaine

substrate: betaine


organism: Listeria monocytogenes

proof_lines:
at 30°C in presence of 300 mM KCl
at 30°C in presence of 600 mM sucrose
at 4°C, no additions


substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP


assay_conditions_summary: 303.15 K; cofactor ATP


assay_conditions_summary: pH 7; cofactor ATP

column_label: PMID 14609945 Table I, wild-type OpuA homodimer row, KM column, glycine betaine uptake in proteoliposomes, KM = 1.9 +/- 0.1 uM.

raw_value_unit_evidence: Table I reports wild-type OpuA homodimer KM = 1.9 +/- 0.1 uM for glycine betaine uptake in proteoliposomes.

row_label: Wild-type OpuA homodimer / glycine betaine uptake

table_label: Table I. Kinetic parameters of glycine betaine uptake in proteoliposomes


organism: Rattus norvegicus


organism: Pseudomonas syringae

assay_conditions_summary: pH 7; buffer containing 0; cofactor ATP

proof_lines: kinetics of OpuC-mediated uptake, in 50 mM of phosphate buffer containing 0.5 M of NaCl, 0.2% glucose, pH 7, low-affinity transport of choline determined


substrate_name: Unknown

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: Unknown


proof_lines:
pH 7.6, 25°C, substrate: MgATP2-
pH 7.6, 25°C, substrate: ammonia
pH 7.6, 25°C, substrate: HCO3-


organism: Sus scrofa

substrate_name: H2O; ATP; CO2; NH3

substrate: H2O; ATP; CO2; NH3


enzyme_display_name: pyruvate kinase

substrate_name: ADP; Phosphoenolpyruvate

enzyme: pyruvate kinase

substrate: ADP; Phosphoenolpyruvate


substrate_name: Phosphoenolpyruvate; ADP

substrate: Phosphoenolpyruvate; ADP


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R336K


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R336Q


sequence_source: UniProtKB/Swiss-Prot accession P0AD61


organism: Arabidopsis thaliana

substrate_name: ADP

substrate: ADP


organism: Ustilago maydis

sequence_source: uniprot

assay_conditions_summary: pH 6.4; cofactor ADP


enzyme_display_name: acid phosphatase

substrate_name: ribose 5-phosphate

assay_conditions_summary: pH 6; 310.15 K; buffer 20 mM sodium acetate

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row Ribose-5-P; column K M (AM) raw value 980 uM; column k cat (s -1) raw value 4.9; column k cat/K M (M -1 s -1) printed 5.0 x 10^3. KM, kcat and the ratio all come from this single table row.

normalized_value_unit_evidence: KM 980 uM = 0.98 mM; kcat 4.9 s^-1; kcat/KM = 4.9 / 0.98 = 5.000000000000001 s^-1 mM^-1 (the table's printed 5.0 x 10^3 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row Ribose-5-P: KM 980 uM; kcat 4.9 s^-1; kcat/KM 5.0 x 10^3 M^-1 s^-1.

enzyme: acid phosphatase

substrate: ribose 5-phosphate


substrate_name: glucose 6-phosphate

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row Glucose-6-P; column K M (AM) raw value 1288 uM; column k cat (s -1) raw value 10; column k cat/K M (M -1 s -1) printed 7.8 x 10^3. KM, kcat and the ratio all come from this single table row.

normalized_value_unit_evidence: KM 1288 uM = 1.288 mM; kcat 10 s^-1; kcat/KM = 10 / 1.288 = 7.763975155279503 s^-1 mM^-1 (the table's printed 7.8 x 10^3 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row Glucose-6-P: KM 1288 uM; kcat 10 s^-1; kcat/KM 7.8 x 10^3 M^-1 s^-1.

substrate: glucose 6-phosphate


substrate_name: Uridine 3'-phosphate

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row 3V-UMP; column K M (AM) raw value 1.2 uM normalizes to 0.0012 mM rather than the exported 0.001 mM; column k cat (s -1) raw value 61 matches; the same-row ratio is 61 / 0.0012 = 50833.333333333336 s^-1 mM^-1 rather than the exported 61000.0 s^-1 mM^-1, and the table prints 5.1 x 10^7 M^-1 s^-1 for this row.

normalized_value_unit_evidence: KM 1.2 uM = 0.0012 mM; kcat 61 s^-1; kcat/KM = 61 / 0.0012 = 50833.333333333336 s^-1 mM^-1 (the table's printed 5.1 x 10^7 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row 3V-UMP: KM 1.2 uM; kcat 61 s^-1; kcat/KM 5.1 x 10^7 M^-1 s^-1.

substrate: Uridine 3'-phosphate


substrate_name: AMP

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row 5V-AMP; column K M (AM) raw value 3.0 uM; column k cat (s -1) raw value 23; column k cat/K M (M -1 s -1) printed 7.6 x 10^6. KM, kcat and the ratio all come from this single table row.

normalized_value_unit_evidence: KM 3.0 uM = 0.003 mM; kcat 23 s^-1; kcat/KM = 23 / 0.003 = 7666.666666666666 s^-1 mM^-1 (the table's printed 7.6 x 10^6 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row 5V-AMP: KM 3.0 uM; kcat 23 s^-1; kcat/KM 7.6 x 10^6 M^-1 s^-1.

substrate: AMP


substrate_name: CMP

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row 5V-CMP; column K M (AM) raw value 138 uM; column k cat (s -1) raw value 26; column k cat/K M (M -1 s -1) printed 1.9 x 10^5. KM, kcat and the ratio all come from this single table row.

normalized_value_unit_evidence: KM 138 uM = 0.138 mM; kcat 26 s^-1; kcat/KM = 26 / 0.138 = 188.40579710144925 s^-1 mM^-1 (the table's printed 1.9 x 10^5 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row 5V-CMP: KM 138 uM; kcat 26 s^-1; kcat/KM 1.9 x 10^5 M^-1 s^-1.

substrate: CMP


substrate_name: 2'-Deoxyguanosine 3'-phosphate

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row 3V-dGMP; column K M (AM) raw value 1.6 uM normalizes to 0.0016 mM rather than the exported 0.002 mM; column k cat (s -1) raw value 26 matches; the same-row ratio is 26 / 0.0016 = 16250.0 s^-1 mM^-1 rather than the exported 13000.0 s^-1 mM^-1, and the table prints 1.6 x 10^7 M^-1 s^-1 for this row.

normalized_value_unit_evidence: KM 1.6 uM = 0.0016 mM; kcat 26 s^-1; kcat/KM = 26 / 0.0016 = 16250.0 s^-1 mM^-1 (the table's printed 1.6 x 10^7 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row 3V-dGMP: KM 1.6 uM; kcat 26 s^-1; kcat/KM 1.6 x 10^7 M^-1 s^-1.

substrate: 2'-Deoxyguanosine 3'-phosphate


substrate_name: 2'-Deoxyuridine 3'-phosphate

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row 3V-dUMP; column K M (AM) raw value 0.9 uM; column k cat (s -1) raw value 29; column k cat/K M (M -1 s -1) printed 3.2 x 10^7. KM, kcat and the ratio all come from this single table row.

normalized_value_unit_evidence: KM 0.9 uM = 0.0009 mM; kcat 29 s^-1; kcat/KM = 29 / 0.0009 = 32222.222222222223 s^-1 mM^-1 (the table's printed 3.2 x 10^7 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row 3V-dUMP: KM 0.9 uM; kcat 29 s^-1; kcat/KM 3.2 x 10^7 M^-1 s^-1.

substrate: 2'-Deoxyuridine 3'-phosphate


substrate_name: Glycerol 2-phosphate

smiles: O=P(O)(O)OC(CO)CO

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row h-Glycerol-P; column K M (AM) raw value 666 uM; column k cat (s -1) raw value 2.9; column k cat/K M (M -1 s -1) printed 4.3 x 10^3. KM, kcat and the ratio all come from this single table row.

normalized_value_unit_evidence: KM 666 uM = 0.666 mM; kcat 2.9 s^-1; kcat/KM = 2.9 / 0.666 = 4.354354354354354 s^-1 mM^-1 (the table's printed 4.3 x 10^3 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row h-Glycerol-P: KM 666 uM; kcat 2.9 s^-1; kcat/KM 4.3 x 10^3 M^-1 s^-1.

row_label: h-Glycerol-P

substrate: Glycerol 2-phosphate


enzyme_display_name: Class B acid phosphatase

substrate_name: dAMP

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row 5V-dAMP; column K M (AM) raw value 0.8 uM; column k cat (s -1) raw value 14; column k cat/K M (M -1 s -1) printed 1.8 x 10^7. KM, kcat and the ratio all come from this single table row.

normalized_value_unit_evidence: KM 0.8 uM = 0.0008 mM; kcat 14 s^-1; kcat/KM = 14 / 0.0008 = 17500.0 s^-1 mM^-1 (the table's printed 1.8 x 10^7 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row 5V-dAMP: KM 0.8 uM; kcat 14 s^-1; kcat/KM 1.8 x 10^7 M^-1 s^-1.

enzyme: Class B acid phosphatase

substrate: dAMP


substrate_name: dGMP

column_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters; row 5V-dGMP; column K M (AM) raw value 3.0 uM; column k cat (s -1) raw value 15; column k cat/K M (M -1 s -1) printed 5.0 x 10^6. KM, kcat and the ratio all come from this single table row.

normalized_value_unit_evidence: KM 3.0 uM = 0.003 mM; kcat 15 s^-1; kcat/KM = 15 / 0.003 = 5000.0 s^-1 mM^-1 (the table's printed 5.0 x 10^6 M^-1 s^-1 is the same quantity at two significant figures).

raw_value_unit_evidence: Table 1 row 5V-dGMP: KM 3.0 uM; kcat 15 s^-1; kcat/KM 5.0 x 10^6 M^-1 s^-1.

substrate: dGMP


substrate_name: 4-Nitrophenyl phosphate

column_label: Table 1 literal pNPP row; Km column 169 μM; kcat column 156 s^-1; printed efficiency column 9.2 × 10^5 M^-1 s^-1. Methods define pNPP as p-nitrophenyl phosphate.

normalized_value_unit_evidence: Km=0.169 mM; kcat=156 s^-1; current same-row quotient=923.076923076923 s^-1 mM^-1; printed efficiency=920 s^-1 mM^-1 and is preserved separately.

raw_value_unit_evidence: pNPP row: Km 169 μM; kcat 156 s^-1; printed kcat/Km 9.2 × 10^5 M^-1 s^-1.

row_label: pNPP

table_label: Table 1. Kinetic parameters of the AphA protein with several organic phosphoesters

substrate: 4-Nitrophenyl phosphate


substrate_name: dUMP

column_label: Table 1 literal 5'-dUMP row and its three metric columns. Its complete tuple exactly equals the current tuple and uniquely excludes the separate 3'-dUMP row.

normalized_value_unit_evidence: Km=0.010 mM; kcat=24 s^-1; same-row quotient and printed efficiency both normalize to 2400 s^-1 mM^-1. The 3'-dUMP row is 0.9 μM/29/3.2 × 10^7 and is excluded.

raw_value_unit_evidence: 5'-dUMP row: Km 10 μM; kcat 24 s^-1; printed kcat/Km 2.4 × 10^6 M^-1 s^-1.

substrate: dUMP


substrate_name: 2'-Deoxyadenosine 3'-phosphate

column_label: Table 1 literal 3'-dAMP row; Km column 1.5 μM; kcat column 27 s^-1; efficiency column 1.8 × 10^7 M^-1 s^-1. The current source is explicitly the 3'-phosphate isomer.

normalized_value_unit_evidence: Paper Km=0.0015 mM, kcat=27 s^-1, and same-row quotient=18000 s^-1 mM^-1. Current Km=0.002 mM and current quotient=13500; both disagree beyond printed precision.

raw_value_unit_evidence: 3'-dAMP row: Km 1.5 μM; kcat 27 s^-1; printed kcat/Km 1.8 × 10^7 M^-1 s^-1.

substrate: 2'-Deoxyadenosine 3'-phosphate


substrate_name: AMP; H2O

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

substrate: AMP; H2O


substrate_name: GMP

substrate: GMP


substrate_name: Cytidine 3'-phosphate

substrate: Cytidine 3'-phosphate


substrate_name: H2O; 4-Nitrophenyl phosphate

substrate: H2O; 4-Nitrophenyl phosphate


substrate_name: GTP

column_label: Table 2; row GTP; column kcat (s^-1) raw value 113; column Km (mM) raw value 0.260; column kcat/Km raw value 434

normalized_value_unit_evidence: kcat normalized_value=113 normalized_unit=s^-1; Km normalized_value=0.260 normalized_unit=mM; kcat/Km normalized_value=434 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=113 raw_unit=s^-1; Km raw_value=0.260 raw_unit=mM; kcat/Km raw_value=434 raw_unit=s^-1*mM^-1

row_label: GTP

table_label: Table 2. Substrate specificity of osteoclastoma tartrate-resistant acid phosphatase

substrate: GTP


substrate_name: Phenolic phosphate

column_label: PMID 2775236 Table 2, page 606; columns kcat (s^-1), Km (mM), and kcat/Km (s^-1 mM^-1); row Phenyl phosphate (source substrate label: Phenolic phosphate; source SMILES matches phenyl phosphate); cells kcat=62, Km=0.606, kcat/Km=102.

raw_value_unit_evidence: Table 2 row Phenyl phosphate (source substrate label: Phenolic phosphate; source SMILES matches phenyl phosphate): kcat=62 s^-1; Km=0.606 mM; kcat/Km=102 s^-1 mM^-1 in the explicit kcat/Km column.

substrate: Phenolic phosphate


column_label: Table 2; row p-Nitrophenylphosphate; column kcat (s^-1) raw value 198; column Km (mM) raw value 1.000; column kcat/Km raw value 198

normalized_value_unit_evidence: kcat normalized_value=198 normalized_unit=s^-1; Km normalized_value=1.000 normalized_unit=mM; kcat/Km normalized_value=198 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=198 raw_unit=s^-1; Km raw_value=1.000 raw_unit=mM; kcat/Km raw_value=198 raw_unit=s^-1*mM^-1

row_label: p-Nitrophenylphosphate


substrate_name: Phosphoenolpyruvate

substrate: Phosphoenolpyruvate


substrate_name: CDP

column_label: Table 2; row CDP; column kcat (s^-1) raw value 58; column Km (mM) raw value 0.606; column kcat/Km raw value 96

normalized_value_unit_evidence: kcat normalized_value=58 normalized_unit=s^-1; Km normalized_value=0.606 normalized_unit=mM; kcat/Km normalized_value=96 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=58 raw_unit=s^-1; Km raw_value=0.606 raw_unit=mM; kcat/Km raw_value=96 raw_unit=s^-1*mM^-1

row_label: CDP

substrate: CDP


substrate_name: Phenolphthalein diphosphate

column_label: Table 2; row Phenolphthalein diphosphate; column kcat (s^-1) raw value 109; column Km (mM) raw value 0.276; column kcat/Km raw value 394

normalized_value_unit_evidence: kcat normalized_value=109 normalized_unit=s^-1; Km normalized_value=0.276 normalized_unit=mM; kcat/Km normalized_value=394 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=109 raw_unit=s^-1; Km raw_value=0.276 raw_unit=mM; kcat/Km raw_value=394 raw_unit=s^-1*mM^-1

row_label: Phenolphthalein diphosphate

substrate: Phenolphthalein diphosphate


substrate_name: dTTP

column_label: Table 2; row TTP; column kcat (s^-1) raw value 107; column Km (mM) raw value 0.299; column kcat/Km raw value 358

normalized_value_unit_evidence: kcat normalized_value=107 normalized_unit=s^-1; Km normalized_value=0.299 normalized_unit=mM; kcat/Km normalized_value=358 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=107 raw_unit=s^-1; Km raw_value=0.299 raw_unit=mM; kcat/Km raw_value=358 raw_unit=s^-1*mM^-1

row_label: TTP

substrate: dTTP


assay_conditions_summary: pH 7.5; 303.15 K; cofactor FMN


substrate_name: H2O; Riboflavin-5-phosphate

assay_conditions_summary: cofactor FMN

proof_lines: SABIO-RK modifier species: acid phosphatase(Enzyme) mutant AtFHy (N-terminal 1-234)

substrate: H2O; Riboflavin-5-phosphate


substrate_name: phosphoenolpyruvate

substrate: phosphoenolpyruvate


substrate_name: myo-inositol hexakisphosphate

substrate: myo-inositol hexakisphosphate


substrate_name: 4-nitrophenyl phosphate

substrate: 4-nitrophenyl phosphate


source_license: CC BY-NC-ND 4.0


substrate_name: dCMP

column_label: Table 1 literal 5'-dCMP row and its three metric columns. Its normalized components equal the current tuple and uniquely exclude the 3'-dCMP row.

normalized_value_unit_evidence: Km=0.035 mM; kcat=26 s^-1; current same-row quotient=742.8571428571428 s^-1 mM^-1; printed efficiency=740 and is retained separately. The distinct 3'-dCMP tuple is excluded by exact row identity.

raw_value_unit_evidence: 5'-dCMP row: Km 35 μM; kcat 26 s^-1; printed kcat/Km 7.4 × 10^5 M^-1 s^-1.

substrate: dCMP


substrate_name: UDP

sequence_source: UniProt REST FASTA

substrate: UDP


substrate_name: 4-Methylumbelliferyl phosphate

substrate: 4-Methylumbelliferyl phosphate


substrate_name: TDP

substrate: TDP


substrate_name: UTP

substrate: UTP


substrate_name: ATP

assay_conditions_summary: pH 5.7; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: alpha-Naphthyl phosphate

substrate: alpha-Naphthyl phosphate


substrate_name: ADP

assay_conditions_summary: pH 5.7; 298.15 K; cofactor ADP

substrate: ADP


substrate_name: H2O; alpha-Naphthyl phosphate

substrate: H2O; alpha-Naphthyl phosphate


substrate_name: p-nitrophenyl phosphate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=4.7

substrate: p-nitrophenyl phosphate


organism: Ipomoea batatas

substrate_name: H2O; 4-Nitrophenyl phosphate

assay_conditions_summary: cofactor ATP

substrate: H2O; 4-Nitrophenyl phosphate


organism: Legionella pneumophila


organism: Pasteurella multocida

column_label: PMC full-text Table 2 row pNPP, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 M^-1); assay conditions in Enzyme activity assays section.

normalized_value_unit_evidence: kcat=6.2 s^-1; Km=0.5 mM; kcat/Km=12 s^-1 mM^-1 from explicit paper kcat/Km 12000 M^-1 s^-1.

raw_value_unit_evidence: pNPP row reports Km 0.5 mM, kcat 6.2 s^-1, kcat/Km 12000 M^-1 s^-1.

table_label: PMC Table 2, Kinetic parameters for rPmCCAP


column_label: PMC full-text Table 2 row 5'-AMP, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 M^-1); assay conditions in Enzyme activity assays section.

normalized_value_unit_evidence: kcat=0.18 s^-1; Km=0.08 mM; kcat/Km=2.3 s^-1 mM^-1 from explicit paper kcat/Km 2300 M^-1 s^-1.

raw_value_unit_evidence: 5'-AMP row reports Km 0.08 mM, kcat 0.18 s^-1, kcat/Km 2300 M^-1 s^-1.


substrate_name: NMN

column_label: PMC full-text Table 2 row NMN, columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 M^-1); assay conditions in Enzyme activity assays section.

normalized_value_unit_evidence: kcat=4.4 s^-1; Km=0.29 mM; kcat/Km=15 s^-1 mM^-1 from explicit paper kcat/Km 15000 M^-1 s^-1.

raw_value_unit_evidence: NMN row reports Km 0.29 mM, kcat 4.4 s^-1, kcat/Km 15000 M^-1 s^-1.

row_label: NMN

substrate: NMN


sequence_source: UniProt FASTA (B9VWB2)


organism: Phaseolus vulgaris

sequence_source: UniProt FASTA (P80366)


organism: Salmonella typhimurium

substrate_name: 4-Nitrophenyl phosphate

sequence_source: UniProt FASTA (Q540U1); residue 154 reconstructed to Arg

substrate: 4-Nitrophenyl phosphate


sequence_source: UniProt FASTA (Q540U1)


substrate_name: 4-Nitrophenyl phosphate; H2O

proof_lines: SABIO-RK modifier species: acid phosphatase(Enzyme) mutant K154N

substrate: 4-Nitrophenyl phosphate; H2O


proof_lines: SABIO-RK modifier species: acid phosphatase(Enzyme) mutant K154R


proof_lines: SABIO-RK modifier species: acid phosphatase(Enzyme) mutant D173N


substrate_name: UMP; H2O

substrate: UMP; H2O


organism: Solanum lycopersicum


substrate_name: Fmoc-EEY(P)AA

proof_lines:
Raw SKiD Env: Temp=25°C, pH=4.9
Raw SKiD Env: Temp=25°C, pH=2.5

substrate: Fmoc-EEY(P)AA


substrate_name: 2'-Deoxycytidine 3'-phosphate

column_label: Public Tor Vergata PDF Table 1 row 3'-dCMP, columns KM=1.3 uM, kcat=101 s^-1, kcat/KM=7.7 x 10^7 M^-1 s^-1.

normalized_value_unit_evidence: KM 0.0013 mM; kcat 101 s^-1; kcat/KM 77000 s^-1 mM^-1; exported KM is 0.001 mM and exported kcat/KM is 101000 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 3'-dCMP cells: KM 1.3 uM; kcat 101 s^-1; kcat/KM 7.7 x 10^7 M^-1 s^-1.

substrate: 2'-Deoxycytidine 3'-phosphate


substrate_name: Guanosine 3'-phosphate

column_label: Public Tor Vergata PDF Table 1 row 3'-GMP, columns KM=1.7 uM, kcat=39 s^-1, kcat/KM=2.3 x 10^7 M^-1 s^-1.

normalized_value_unit_evidence: KM 0.0017 mM; kcat 39 s^-1; kcat/KM 23000 s^-1 mM^-1; exported KM is 0.002 mM and exported kcat/KM is 19500 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 3'-GMP cells: KM 1.7 uM; kcat 39 s^-1; kcat/KM 2.3 x 10^7 M^-1 s^-1.

substrate: Guanosine 3'-phosphate


substrate_name: UMP

column_label: Public Tor Vergata PDF Table 1 row 5'-UMP, columns KM=15 uM, kcat=61 s^-1, kcat/KM=4.1 x 10^6 M^-1 s^-1.

normalized_value_unit_evidence: KM 0.015 mM; kcat 61 s^-1; table kcat/KM 4100 s^-1 mM^-1; exported kcat/KM 4066.666666666667 s^-1 mM^-1 is consistent with recomputing 61 / 0.015 from printed kcat and KM cells.

raw_value_unit_evidence: Table 1 row 5'-UMP cells: KM 15 uM; kcat 61 s^-1; kcat/KM 4.1 x 10^6 M^-1 s^-1.

substrate: UMP


substrate_name: Adenosine 3'-phosphate

column_label: Public Tor Vergata PDF Table 1 row 3'-AMP, columns KM=0.9 uM, kcat=33 s^-1, kcat/KM=4.1 x 10^7 M^-1 s^-1.

raw_value_unit_evidence: Table 1 row 3'-AMP cells: KM 0.9 uM; kcat 33 s^-1; kcat/KM 4.1 x 10^7 M^-1 s^-1.

substrate: Adenosine 3'-phosphate


organism: Glycine max


organism: Haemophilus influenzae

substrate_name: nicotinamide mononucleotide

substrate: nicotinamide mononucleotide


organism: Homo sapiens

substrate_name: GDP

column_label: Table 2; row GDP; column kcat (s^-1) raw value 86; column Km (mM) raw value 0.348; column kcat/Km raw value 246

normalized_value_unit_evidence: kcat normalized_value=86 normalized_unit=s^-1; Km normalized_value=0.348 normalized_unit=mM; kcat/Km normalized_value=246 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=86 raw_unit=s^-1; Km raw_value=0.348 raw_unit=mM; kcat/Km raw_value=246 raw_unit=s^-1*mM^-1

row_label: GDP

substrate: GDP


substrate_name: CTP

column_label: Table 2; row CTP; column kcat (s^-1) raw value 93; column Km (mM) raw value 0.377; column kcat/Km raw value 248

normalized_value_unit_evidence: kcat normalized_value=93 normalized_unit=s^-1; Km normalized_value=0.377 normalized_unit=mM; kcat/Km normalized_value=248 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=93 raw_unit=s^-1; Km raw_value=0.377 raw_unit=mM; kcat/Km raw_value=248 raw_unit=s^-1*mM^-1

row_label: CTP

substrate: CTP


enzyme_display_name: beta-lactamase

organism: Shewanella algae

substrate_name: Ticarcillin

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Ticarcillin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 1, Km 20, kcat/Km 50.

normalized_value_unit_evidence: kcat normalized_value=1 normalized_unit=s^-1; Km normalized_value=0.02 normalized_unit=mM; kcat/Km normalized_value=50 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Ticarcillin: kcat 1 s^-1; Km 20 uM; kcat/Km 50 mM^-1 s^-1; relative kcat/Km 31.

row_label: OXA-55 / Ticarcillin

enzyme: beta-lactamase

substrate: Ticarcillin


substrate_name: cefpirome

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Cefpirome; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 0.1, Km 670, kcat/Km 0.1.

normalized_value_unit_evidence: kcat normalized_value=0.1 normalized_unit=s^-1; Km normalized_value=0.67 normalized_unit=mM; kcat/Km normalized_value=0.1 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Cefpirome: kcat 0.1 s^-1; Km 670 uM; kcat/Km 0.1 mM^-1 s^-1; relative kcat/Km 0.06.

row_label: OXA-55 / Cefpirome

substrate: cefpirome


substrate_name: Cloxacillin

column_label: Table 2. Kinetic parameters and relative kcat/Km values of purified beta-lactamase OXA-55 from S. algae KB-1, OXA-54 from S. oneidensis MR-1, and OXA-40 from A. baumannii CLA-1.; row OXA-55 / Cloxacillin; columns OXA-55 kcat (s^-1), Km (uM), kcat/Km (mM^-1 s^-1); cells kcat 0.5, Km 190, kcat/Km 3.

normalized_value_unit_evidence: kcat normalized_value=0.5 normalized_unit=s^-1; Km normalized_value=0.19 normalized_unit=mM; kcat/Km normalized_value=3 normalized_unit=s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row OXA-55 / Cloxacillin: kcat 0.5 s^-1; Km 190 uM; kcat/Km 3 mM^-1 s^-1; relative kcat/Km 1.5.

row_label: OXA-55 / Cloxacillin

substrate: Cloxacillin


organism: Shewanella frigidimarina

substrate_name: H2O; Amoxicillin

substrate: H2O; Amoxicillin


organism: Shewanella livingstonensis

substrate_name: Amoxicillin; H2O

substrate: Amoxicillin; H2O


organism: Staphylococcus aureus

substrate_name: Cefuroxime

assay_conditions_summary: pH 6; 310.15 K; buffer pH 6

column_label: Same-row type A Cefuroxime cells match exported kcat 0.009 s^-1, Km 0.378 mM, and kcat/Km 0.023809523809523808 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 reports Cefuroxime Km 378 uM for type A; Table 2 reports Cefuroxime kcat 0.009 s^-1 for type A; Table 4 identifies Cefuroxime REH for type A.

row_label: Cefuroxime; beta-lactamase type A (PC1)

table_label: Tables 1, 2, and 4 kinetic constants/REH, PDF pp. 2-3

substrate: Cefuroxime


substrate_name: cefazolin

substrate: cefazolin


substrate_name: Ampicillin

substrate: Ampicillin


assay_conditions_summary: pH 5; 310.15 K; cofactor ATP

proof_lines:
pH 5, 37°C
pH 6.0, 37°C, recombinant enzyme
pH 5.0, 37°C, isoenzyme AP2


substrate_name: phosphoenolpyruvate

assay_conditions_summary: pH 5.4; 310.15 K; cofactor ADP

proof_lines: pH 6.2-6.4, 37°C, trypsin-cleaved recombinant enzyme, in presence of L-ascorbate

substrate: phosphoenolpyruvate


substrate_name: D-sucrose 6-phosphate

proof_lines: pH 4.4, Fe(III)-substituted acid phosphatase

substrate: D-sucrose 6-phosphate


organism: Labeo rohita

substrate_name: 4-nitrophenyl phosphate

proof_lines: pH 5.5, 37°C, isoenzyme 1, Vmax (mmol/min/mg): 0.0093

proof_lines: pH 5.5, 37°C, isoenzyme 1, Vmax (mmol/min/mg): 0.0076

proof_lines: pH 5.5, 37°C, isoenzyme 1, Vmax (mmol/min/mg): 0.0058

substrate: 4-nitrophenyl phosphate


organism: Pinctada fucata

proof_lines:
pH 4.6, 47°C, purified isozyme I
pH 3.2, 57°C, purified isozyme II


organism: Caenorhabditis elegans

substrate_name: alpha-naphthyl phosphate

substrate: alpha-naphthyl phosphate


organism: Escherichia coli (strain K12)

substrate_name: 5'-AMP (at 37 degrees Celsius)

substrate: 5'-AMP (at 37 degrees Celsius)


substrate_name: p-NPP (at pH 5.5 and 25 degrees Celsius)

assay_conditions_summary: pH 5.5; cofactor ATP


organism: Ipomoea batatas

substrate_name: p-NPP (at pH 4.9 and 25 degrees Celsius)


assay_conditions_summary: pH 4.9; cofactor ATP

substrate: p-NPP (at pH 4.9 and 25 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


organism: Arabidopsis thaliana

substrate_name: phosphoenolpyruvate (for the phosphatase activity)


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


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

substrate_name: 5'-UMP (at 37 degrees Celsius and pH 6.5)


organism: Schizophyllum commune

substrate_name: para-nitrophenylphosphate (p-NPP)

sequence: NAPWAQIDEV

wild_type_sequence: NAPWAQIDEV

substrate: para-nitrophenylphosphate (p-NPP)


substrate_name: p-nitrophenyl phosphate (at pH 5.5 and 37 degrees Celsius)

proof_lines: kcat is 0.00071 sec(-1) for phosphoglycerate mutase activity (PubMed:16672613). The enzyme's FBPase activity does not follow Michaelis-Menten kinetics but follows allosteric sigmoidal kinetics that show lower affinity for FBP compared with


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: ATP (at pH 5.5 and 37 degrees Celsius)

proof_lines: kcat is 3.9 min(-1) with ATP as substrate (at pH 5.5 and 37 degrees Celsius) (PubMed:20070315). kcat is 3.8 min(-1) with ATP as substrate (at pH 7 and 37 degrees Celsius) (PubMed:20070315). kcat is 3.0 min(-1) with ADP as substrate (at pH 5

substrate: ATP (at pH 5.5 and 37 degrees Celsius)


organism: Schistosoma mansoni

substrate_name: Phosphoenolpyruvate; ADP

substrate: Phosphoenolpyruvate; ADP


organism: Saccharolobus solfataricus

proof_lines: 50°C, pH not specified in the publication

proof_lines: 65°C, pH not specified in the publication

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


organism: Homo sapiens

substrate_name: phosphoenolpyruvate / ADP

assay_conditions_summary: pH 8; 305.15 K; cofactor ADP

proof_lines: in the presence of D-fructose 1,6-bisphosphate

proof_lines: pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate

substrate: phosphoenolpyruvate / ADP


assay_conditions_summary: pH 7.6; 310.15 K; cofactor ADP


organism: Aspergillus niger


organism: Berryteuthis magister

substrate_name: Phenyl phosphate

substrate: Phenyl phosphate


organism: Blastobotrys adeninivorans

substrate_name: AMP

assay_conditions_summary: pH 4.5; 333.15 K; buffer 100 mM sodium acetate

proof_lines: recombinant enzyme, in 100 mM sodium acetate buffer (pH 4.5), at 60°C

substrate: AMP


organism: Bos taurus

substrate_name: DL-phosphotyrosine

assay_conditions_summary: pH 7

proof_lines:
pH 7
pH 8
pH 9

substrate: DL-phosphotyrosine


organism: Brassica nigra

substrate_name: phosphoenolpyruvate

assay_conditions_summary: cofactor ADP


organism: Candida albicans


organism: Carthamus oxyacanthus

substrate_name: 4-nitrophenyl phosphate


organism: Cicer arietinum


organism: Clostridium perfringens


organism: Cullen corylifolium


organism: Dioscorea cayenensis-rotundata

proof_lines:
cytoplasmic enzyme
enzyme A
enzyme B


organism: Drosophila melanogaster


organism: Vibrio cholerae serotype O1

proof_lines: pH 7.0, 25°C, recombinant non-His-tagged enzyme, in presence of fructose 1,6-bisphosphate

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme, in presence of fructose 1,6-bisphosphate


organism: Allium sativum


organism: Arabidopsis thaliana

substrate_name: sodium phytate

substrate: sodium phytate


organism: Arachis hypogaea

substrate_name: Phenylphosphate

assay_conditions_summary: pH 5; 310.15 K; buffer 100 mM sodium acetate; cofactor ATP

proof_lines: at 37°C in 100 mM sodium acetate buffer (pH 5.0)

substrate: Phenylphosphate


organism: Asclepias curassavica


organism: Aspergillus caespitosus

proof_lines:
pH 5.6, 80°C, intracellular enzyme
pH 5.6, 80°C, extracellular enzyme


organism: Aspergillus nidulans


organism: Eimeria tenella


organism: Entamoeba histolytica

substrate_name: 3-O-methylfluorescein phosphate

proof_lines:
pH 6.0, 37°C, recombinant enzyme
pH 5.5, 37°C

substrate: 3-O-methylfluorescein phosphate


organism: Erythrina variegata

proof_lines: isoform AP-I, pH not specified in the publication, temperature not specified in the publication


organism: Escherichia coli

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


organism: Euphorbia characias


organism: Francisella tularensis

substrate_name: thiamine diphosphate

proof_lines: pH 37°C, pH 5.6, 1 mM MgCl2, Vmax: 1.38 micromol/min/mg

proof_lines: pH 37°C, pH 5.6, 1 mM MgCl2, Vmax: 11.84 micromol/min/mg

proof_lines: pH 37°C, pH 5.6, 1 mM MgCl2, Vmax: 13.3 micromol/min/mg

substrate: thiamine diphosphate


organism: Acidithiobacillus thiooxidans

substrate_name: p-nitrophenyl phosphate


organism: Acinetobacter baumannii


organism: Agaricus bisporus

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Gallus gallus

substrate_name: 4-methylumbelliferyl phosphate

proof_lines:
enzyme form B
enzyme form A

substrate: 4-methylumbelliferyl phosphate


organism: Gossypium hirsutum


organism: Haemophilus influenzae


organism: Helianthus annuus

proof_lines:
enzyme form I
enzyme form II


organism: Helicobacter pylori

proof_lines: pH 6.0, 37°C, periplasmic enzyme with 0.1 mM NiCl2

proof_lines: pH 6.0, 37°C, periplasmic enzyme without Ni2+

substrate: 4-nitrophenyl phosphate


organism: Heterostelium pallidum


organism: Homo sapiens


organism: Hordeum vulgare


organism: Hypericum perforatum


organism: Juglans regia

substrate_name: O-phospho-L-tyrosine

substrate: O-phospho-L-tyrosine


organism: Lactococcus lactis subsp. lactis

substrate_name: 2-Deoxy-D-glucose 6-phosphate; H2O

substrate: 2-Deoxy-D-glucose 6-phosphate; H2O


organism: Lactuca sativa


organism: Legionella micdadei


organism: Legionella pneumophila


organism: Leishmania mexicana

substrate: p-nitrophenyl phosphate


organism: Lens culinaris


organism: Lupinus luteus

substrate_name: H2O; 4-Nitrophenyl phosphate

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

substrate: H2O; 4-Nitrophenyl phosphate


organism: Macrotyloma uniflorum


organism: Mucor hiemalis


organism: Musa acuminata


organism: Musa cavendishii

substrate_name: diphosphate

substrate: diphosphate


organism: Mycolicibacterium smegmatis

proof_lines: at pH 5.5, temperature not specified in the publication

proof_lines: at pH 4.5, temperature not specified in the publication


organism: Nelumbo nucifera


organism: Nicotiana tabacum

substrate_name: RRA(pT)VA

assay_conditions_summary: pH 5.8; 303.15 K; cofactor ATP

substrate: RRA(pT)VA


organism: Nototodarus sloanii

substrate_name: Phenyl phosphate


organism: Opuntia megacantha


organism: Oryctolagus cuniculus

proof_lines:
acidic enzyme form
basic enzyme form


organism: Paracoccus denitrificans


organism: Pasteurella multocida


organism: Pelophylax lessonae

substrate_name: hirudin 53-65 C-terminal fragment

proof_lines: per number of phosphoserine residues, pH 5.0, 37°C

substrate: hirudin 53-65 C-terminal fragment


organism: Phaseolus vulgaris

substrate_name: methylphosphate

proof_lines:
at pH 6.25
recombinant enzyme
at pH 4.9

substrate: methylphosphate


organism: Phoenix canariensis


organism: Pinus sylvestris


organism: Prevotella intermedia


proof_lines: pH 4.9, 37°C, mutant enzyme L51T and P55T


mutation_type: deletion


organism: Pseudomonas aeruginosa

substrate_name: phosphorylcholine

proof_lines:
pH 5.0, 37°C
pH 5.0, 37°C, partially purified enzyme

substrate: phosphorylcholine


organism: Rattus norvegicus


organism: Ribes nigrum


organism: Rumex dentatus

substrate_name: 4-nitrophenyl phosphate


organism: Saccharomyces cerevisiae

substrate_name: thiamine phosphate

proof_lines: thiamine-repressible acid phosphatase, pH 5.0, 37°C

proof_lines: thiamine-repressible acid phosphatase, pH 3.0, 37°C

proof_lines: phosphate-repressible acid phosphatase, pH 4.5, 37°C

substrate: thiamine phosphate


organism: Salmonella enterica subsp. enterica serovar Typhimurium

assay_conditions_summary: pH 5.5; 310.15 K; buffer 100 mM sodium acetate

proof_lines: mutant enzyme I78A, in 100 mM sodium acetate buffer, at 37°C and pH 5.5

proof_lines: mutant enzyme I78A, in 100 mM sodium acetate buffer, at 37°C and pH 8.5

proof_lines: mutant enzyme I78A, in 100 mM sodium acetate buffer, at 37°C and pH 3.5


proof_lines: mutant enzyme I78D, in 100 mM sodium acetate buffer, at 37°C and pH 5.5

proof_lines: mutant enzyme I78D, in 100 mM sodium acetate buffer, at 37°C and pH 8.5

proof_lines: mutant enzyme I78D, in 100 mM sodium acetate buffer, at 37°C and pH 7.0


assay_conditions_summary: pH 8.5; 310.15 K; buffer 100 mM sodium acetate

proof_lines: wild type enzyme, in 100 mM sodium acetate buffer, at 37°C and pH 8.5

proof_lines: wild type enzyme, in 100 mM sodium acetate buffer, at 37°C and pH 3.5

proof_lines: wild type enzyme, in 100 mM sodium acetate buffer, at 37°C and pH 5.5


proof_lines: mutant enzyme I78H, in 100 mM sodium acetate buffer, at 37°C and pH 8.5

proof_lines: mutant enzyme I78H, in 100 mM sodium acetate buffer, at 37°C and pH 7.0

proof_lines: mutant enzyme I78H, in 100 mM sodium acetate buffer, at 37°C and pH 3.5


organism: Schizophyllum commune


organism: Schizosaccharomyces pombe


organism: Secale cereale

substrate_name: fructose 1,6-diphosphate

substrate: fructose 1,6-diphosphate


organism: Secale cereale x Triticum aestivum

substrate_name: ATP

proof_lines:
enzyme from plump seed
enzyme from shriveled seed

substrate: ATP


organism: Selenastrum capricornutum

substrate_name: Unknown

substrate: Unknown


organism: Senna occidentalis

proof_lines:
isoform ACP80, 37°C, pH 5.6
isoform ACP60, 37°C, pH 5.6


organism: Sinorhizobium meliloti


organism: Solanum lycopersicum

substrate_name: GTP

assay_conditions_summary: pH 5.1; 298.15 K; cofactor ATP

substrate: GTP


organism: Solanum tuberosum

assay_conditions_summary: pH 5.6; buffer 75 mM sodium acetate

proof_lines: in 75 mM sodium acetate buffer (pH 5.6), in the absence of polyamine and Mg2+


organism: Sorghum bicolor

substrate: Phenyl phosphate


organism: Sphingobium sp. RSMS


organism: Staphylococcus aureus

substrate_name: p-nitrophenyl phosphate


organism: Sulfolobus acidocaldarius

proof_lines:
pH 5.0, 50°C
in 50 mM Na-acetate (pH 5.0), at 50°C


organism: Sus scrofa


organism: Talaromyces funiculosus


organism: Tetradesmus obliquus


organism: Tetrahymena pyriformis


organism: Thermus thermophilus


organism: Trichoderma harzianum


organism: Triticum aestivum


organism: Trypanosoma brucei


organism: Trypanosoma brucei brucei


organism: Ustilago esculenta


organism: Vigna aconitifolia

assay_conditions_summary: pH 5; 303.15 K; cofactor ADP

proof_lines: pH 5.0, 37°C, enzyme immobilized onto chitosan beads


organism: Vigna mungo


organism: Yarrowia lipolytica


organism: Zea mays

proof_lines: enzyme purified from 72h-old scutellum tissue

proof_lines: enzyme purified from 10h-old scutellum tissue


organism: Pseudomonas fluorescens

substrate_name: Oxacillin

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)

substrate: Oxacillin


organism: Psychrobacter immobilis

substrate_name: ampicillin

substrate: ampicillin


organism: Enterobacter cloacae


substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


organism: Escherichia coli

substrate_name: Cephalothin

substrate: Cephalothin


organism: Fluoribacter gormanii

substrate_name: cefotaxime

column_label: Table II columns under [Zn2+] = 100 uM: kcat [s^-1], Km [uM], kcat/Km [uM^-1 s^-1]; WT Cefotaxime cells 430, 70, 6.1.

normalized_value_unit_evidence: Km 70 uM = 0.07 mM; kcat 430 s^-1; printed kcat/Km 6.1 uM^-1 s^-1 = 6100 s^-1 mM^-1; expected computed ratio 6142.857142857142 s^-1 mM^-1 is within table precision/rounding.

raw_value_unit_evidence: Table II WT Cefotaxime at [Zn2+] = 100 uM: kcat 430 s^-1, Km 70 uM, kcat/Km 6.1 uM^-1 s^-1.

row_label: WT / Cefotaxime

table_label: JBC official article HTML Table II, Kinetic parameters of the wild type enzyme (WT) and mutant FEZ-1 enzymes

substrate: cefotaxime


organism: Morganella morganii

substrate_name: Cefotaxime

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant M37

substrate: Cefotaxime


substrate_name: Penicillin G

substrate: Penicillin G


organism: Mycobacterium tuberculosis

substrate_name: Nitrocefin

substrate: Nitrocefin


organism: Acinetobacter baumannii

substrate_name: benzylpenicillin (at pH 7.0 and 30 degrees Celsius)

proof_lines: kcat is 5.5 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:15616297). kcat is 106 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:26459904). kcat is 1 sec(-1) with


proof_lines: kcat is 460 sec(-1) for ampicillin (at pH 7.4 and 25 degrees Celsius, in the presence of 0.025 M NaHCO3) (PubMed:23877677). kcat is 580 sec(-1) for ampicillin (at pH 7.0, in the presence of 0.05 M NaHCO3) (PubMed:30530607). kcat is 0.49 sec


organism: Aeromonas hydrophila

substrate_name: cefuroxime

proof_lines: kcat is 1200 sec(-1) for lactamase activity with imipenem as substrate (PubMed:15588826, PubMed:19651913). kcat is 300 sec(-1) for lactamase activity with biapenem as substrate (PubMed:15588826). kcat is 210 sec(-1) for lactamase activity w

substrate: cefuroxime


organism: Bacteroides fragilis

substrate_name: nitrocefin (with zinc ions at pH 7 and 25 degrees Celsius)

proof_lines: kcat is 225.7 sec(-1) for lactamase activity with nitrocefin as substrate (with zinc ions at pH 7 and 25 degrees Celsius). kcat is 107.6 sec(-1) for lactamase activity with nitrocefin as substrate (with cobalt ions at pH 7 and 25 degrees Ce


organism: Citrobacter amalonaticus

substrate_name: benzylpenicillin

proof_lines: Value for ceftazidime was determined as Ki by substrate competition with benzylpenicillin.

substrate: benzylpenicillin


organism: Elizabethkingia meningoseptica

substrate_name: cefoxitin

proof_lines: kcat is 350 sec(-1) for lactamase activity with imipenem as substrate. kcat is 300 sec(-1) for lactamase activity with 6-beta-iodopenicillanate as substrate. kcat is 280 sec(-1) for lactamase activity with penicillin G as substrate. kcat is

substrate: cefoxitin


organism: Klebsiella pneumoniae

proof_lines: kcat is 245 sec(-1) with benzylpenicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:14693513). kcat is 340 sec(-1) with ampicillin as substrate (at pH 7.0 and 30 degrees Celsius) (PubMed:14693513). kcat is 208 sec(-1) with amp

substrate: benzylpenicillin (at pH 7.0 and 30 degrees Celsius)


organism: Treponema pallidum

substrate_name: Penicillin G; H2O; Penicillin G; H2O; Substituted beta-amino acid; H2O; Carbenicillin; Carbenicillin; Oxacillin; H2O; Oxacillin; H2O; Cloxacillin; Cloxacillin; 6-alpha-Hydroxymethylpenicillanate; H2O; 6-alpha-Hydroxymethylpenicillanate


organism: Bacillus licheniformis

substrate_name: Penicillin V; H2O

substrate: Penicillin V; H2O


substrate_name: H2O; Penicillin G

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105W

substrate: H2O; Penicillin G


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant Y105N


substrate_name: H2O; Ampicillin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244E

substrate: H2O; Ampicillin


sequence_source: UniProt REST accession Q6XEC0 sequence

column_label: Chemistry & Biology 2009 Table 1, row label Ampicillin; kcat_over_km paper=2400 s^-1 mM^-1; export=2417.721518987342 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=955 s^-1; km=0.395 mM; kcat_over_km=2400 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Ampicillin; kcat 955 s^-1; Km 395 uM; kcat/Km 2.4 x 10^6 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.

row_label: Ampicillin

table_label: Chemistry & Biology 2009 Table 1


substrate_name: Oxacillin

column_label: Chemistry & Biology 2009 Table 1, row label Oxacillin; kcat_over_km paper=1400 s^-1 mM^-1; export=1368.421052631579 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=130 s^-1; km=0.095 mM; kcat_over_km=1400 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Oxacillin; kcat 130 s^-1; Km 95 uM; kcat/Km 1.4 x 10^6 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.

row_label: Oxacillin


substrate_name: temocillin

column_label: Official Cell fulltext HTML Table 1 row Temocillin columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row Temocillin: kcat 0.3 s^-1; Km 45 uM; kcat/Km 6.6 x 10^3 M^-1 s^-1.

row_label: Temocillin

table_label: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates

substrate: temocillin


substrate_name: faropenem

column_label: Official Cell fulltext HTML Table 1 row Faropenem columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row Faropenem: kcat 0.038 s^-1; Km 13 uM; kcat/Km 2.9 x 10^3 M^-1 s^-1.

row_label: Faropenem

substrate: faropenem


substrate_name: ertapenem

column_label: Official Cell fulltext HTML Table 1 row Ertapenem columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

normalized_value_unit_evidence: kcat 0.13 s^-1; Km 0.1 mM; metric-labeled kcat/Km 1.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row Ertapenem: kcat 0.13 s^-1; Km 100 uM; kcat/Km 1.3 x 10^3 M^-1 s^-1.

row_label: Ertapenem

substrate: ertapenem


substrate_name: nitrocefin

column_label: Chemistry & Biology 2009 Table 1, row label Nitrocefin; kcat_over_km paper=7700 s^-1 mM^-1; export=7833.333333333334 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=940 s^-1; km=0.12 mM; kcat_over_km=7700 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Nitrocefin; kcat 940 s^-1; Km 120 uM; kcat/Km 7.7 x 10^6 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.

row_label: Nitrocefin

substrate: nitrocefin


substrate_name: Imipenem

column_label: Chemistry & Biology 2009 Table 1, row label Imipenem; kcat_over_km paper=370 s^-1 mM^-1; export=369.2307692307692 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=4.8 s^-1; km=0.013 mM; kcat_over_km=370 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Imipenem; kcat 4.8 s^-1; Km 13 uM; kcat/Km 3.7 x 10^5 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%.

row_label: Imipenem

substrate: Imipenem


substrate_name: cephalothin

column_label: Chemistry & Biology 2009 Table 1, row label Cephalothin (footnote a); kcat_over_km paper=230 s^-1 mM^-1; export=225.64102564102564 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=44 s^-1; km=0.195 mM; kcat_over_km=230 s^-1 mM^-1.

raw_value_unit_evidence: Table 1. Kinetic Parameters of Oxa-48 with Representative beta-Lactam Substrates; row Cephalothin (footnote a); kcat 44 s^-1; Km 195 uM; kcat/Km 2.3 x 10^5 M^-1 s^-1. Values calculated on the basis of three independent experiments; SDs were below 10%. Footnote for this substrate: Biphasic kinetics were observed with this substrate. However, the rapid establishment of the steady state did not allow the measurement of initial rate kinetic parameters.

row_label: Cephalothin (footnote a)

substrate: cephalothin


substrate_name: H2O; Nitrocefin

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant G238S

substrate: H2O; Nitrocefin


substrate_name: Ampicillin; H2O

proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244S

substrate: Ampicillin; H2O


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244Q


proof_lines: SABIO-RK modifier species: beta-lactamase(Enzyme) mutant SHV-1 R244L


enzyme_display_name: carbonic anhydrase

organism: Candida albicans

substrate_name: CO2; H2O

enzyme: carbonic anhydrase

substrate: CO2; H2O


organism: Cryptococcus neoformans

substrate_name: H2O; CO2

substrate: H2O; CO2


organism: Homo sapiens


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant N62V


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant N62T


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant N62D


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant N62A


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant T199D


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant T199H


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant T199E


organism: Bos taurus

proof_lines:
pH 8-9, 25°C
at pH 7.0 and 20°C
pH 7.4, 20°C, cytosolic isoenzyme


organism: Brucella suis

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

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

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

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


organism: Elephas trogontherii

substrate_name: p-nitrophenyl acetate

proof_lines:
integral isoenzyme
inner peripheral isoenzyme
outer peripheral isoenzyme

substrate: p-nitrophenyl acetate


organism: Helicobacter pylori

proof_lines:
pH 8.9, 25°C
isoenzyme hpalphaCA
isoenzyme hpbetaCA


assay_conditions_summary: pH 6.3; 298.15 K; buffer conditions

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


organism: Mus musculus

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


enzyme_display_name: Carbonic anhydrase, chloroplastic

organism: Spinacia oleracea

substrate_name: Dihydrogen carbonate

smiles: O=C(O)O

enzyme: Carbonic anhydrase, chloroplastic

substrate: Dihydrogen carbonate


enzyme_display_name: Carbonic anhydrase

organism: Synechocystis sp. PCC 6803 / Kazusa

enzyme: Carbonic anhydrase


organism: Stylophora pistillata

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

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

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

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


organism: Solanum tuberosum

proof_lines:
chloroplastic isoenzyme
cytosolic isoenzyme


organism: Methanosarcina thermophila

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


organism: Bacillus cereus

substrate_name: Penicillin G

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04190 and applied mutation signature H116S to reconstruct the assayed variant sequence.

column_label: Table 3 (kinetic parameters with respect to benzylpenicillin and nitrocefin, 10 mM Hepes/0.2 M NaCl, pH 7.5, 30 C), enzyme row 'H116S', benzylpenicillin column group; column 'Km (uM)' = 530; column 'kcat (s^-1)' = 47; column 'kcat/Km (M^-1 s^-1)' = 89000.

normalized_value_unit_evidence: Km: printed Table 3 cell 530 uM; 530 / 1000 = 0.53 mM; the paper value is 0.53 mM and the exported value is 0.53 mM. kcat: printed Table 3 cell 47 s^-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 47.0 s^(-1) and the exported value is 47.0 s^(-1). kcat/Km: printed Table 3 cell 89000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 89000 / 1000 = 89.0 s^-1 mM^-1; the paper value is 89.0 s^(-1)*mM^(-1); the exported value is 88.67924528301886 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme row 'H116S', benzylpenicillin column group: Km = 530 uM; kcat = 47 s^-1; printed kcat/Km = 89000 M^-1 s^-1.

table_label: Table 3: Kinetic parameters with respect to benzylpenicillin and nitrocefin for the enzyme forms of Bacillus cereus 569/H/9 metallo-beta-lactamase BcII in 10 mM Hepes/0.2 M NaCl at pH 7.5 and 30 C (Biochem. J. 2002, 363:687-696)

substrate: Penicillin G


organism: Dioscorea japonica

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

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


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

assay_conditions_summary: pH 8

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


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

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


organism: Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)

substrate_name: Unknown

proof_lines: kcat is 8700 sec(-1) at pH 8.5, from purified carboxysomes.

substrate: Unknown


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 940000 sec(-1) with CO(2) as substrate.


organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)

proof_lines: kcat is 3340 sec(-1) for full length enzyme at pH 7.5.


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


organism: Homo sapiens


organism: Methanosarcina thermophila (strain ATCC 43570 / DSM 1825 / OCM 12 / VKM B-1830 / TM-1)


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


organism: Persephonella marina (strain DSM 14350 / EX-H1)


organism: Escherichia coli


organism: Pseudomonas putida

substrate_name: carbenicillin

assay_conditions_summary: buffer / inhibitor assay context

proof_lines: enzyme diluted in HEPES buffer containing 50 microM ZnCl2 supplemented with bovine serum albumin

proof_lines: inhibitor binding constant (Ki) using 10 microM nitrocefin as indicator substrate

substrate: carbenicillin


organism: Pseudomonas fluorescens

substrate_name: Oxacillin

assay_conditions_summary: pH 7; 303.15 K; buffer sodium phosphate

proof_lines: at 30°C in 50mM sodium phosphate buffer (pH 7.0)

substrate: Oxacillin


organism: Acipenser gueldenstaedtii

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

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


organism: Cryptococcus neoformans

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

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

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


organism: Cyprinus carpio


organism: Danio rerio

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


organism: Drosophila melanogaster

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


organism: Dunaliella salina

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


organism: Entamoeba histolytica


organism: Enterobacter sp. B13

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


organism: Felis catus

assay_conditions_summary: pH 6

proof_lines:
pH 6-8
above pH 8


organism: Flaveria bidentis


organism: Gyrodactylus salaris


organism: Halomonas sp.

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


organism: Clostridium perfringens

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


organism: Coccomyxa sp.


organism: Columba livia


organism: Colwellia psychrerythraea

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


organism: Conticribra weissflogii

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

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


organism: Corynebacterium flavescens

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Aedes aegypti


organism: Anguilla anguilla


organism: Arabidopsis thaliana


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant H216N


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant Y212F


proof_lines: SABIO-RK modifier species: carbonate dehydratase(Enzyme) mutant Q158A


organism: Shouchella clausii

substrate_name: cefoxitin

proof_lines: kcat less than 0.01/sec at 30°C in 100 mM sodium phosphate (pH 7)

proof_lines: kcat less than 0.3/sec at 30°C in 100 mM sodium phosphate (pH 7)

substrate: cefoxitin


organism: Halothiobacillus neapolitanus

assay_conditions_summary: pH 7

proof_lines:
pH 7.0, rCsoSCA
rCsoSCA


organism: Homo sapiens


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


assay_conditions_summary: pH 6.28; buffer text plus the mutant label

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

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

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


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


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


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

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

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


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

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

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


organism: Astrosclera willeyana


organism: Bacillus subtilis

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

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


organism: Caenorhabditis elegans

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


organism: Candida albicans

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

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

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


organism: Cavia porcellus

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

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


organism: Chionodraco hamatus


organism: Lathyrus oleraceus


organism: Leishmania chagasi


organism: Macropus eugenii desmarest


organism: Malassezia globosa


organism: Malassezia pachydermatis

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


organism: Malassezia restricta


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

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

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


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


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

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

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


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


organism: Lacticaseibacillus rhamnosus


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


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


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


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

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

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


organism: Methanosarcina thermophila

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

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


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


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


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


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


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


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


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


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


organism: Methanothermobacter thermautotrophicus

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


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


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


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

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

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


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


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


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


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


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


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


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


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


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


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

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


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


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

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


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


organism: Micropterus salmoides


organism: Mus musculus


proof_lines:
pH 9.0, 25°C, mutant R94H/E92Q
pH 7.0, 10°C, double mutant R94H/E92Q


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

mutation_type: truncation


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


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

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


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

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

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


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


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

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


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


organism: Ovis aries

proof_lines:
Vmax: 0.168 micromol/min, pH 8.5, 35°C
pH 8.5, 35°C
pH 7.4, 25°C, purified enzyme


organism: Persephonella marina

proof_lines:
pH 7.5, 20°C
pH 7.8, 25°C, recombinant enzyme


organism: Petromyzon marinus


organism: Petroselinum crispum

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


organism: Plasmodium falciparum

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

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


mutation_signature: truncated mutant PfCA1


organism: Neisseria gonorrhoeae


organism: Nostoc commune

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


organism: Nostoc sp.


organism: Oncorhynchus mykiss

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

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


organism: Oryctolagus cuniculus

proof_lines: enzyme from red muscle sarcoplasmic reticulum

proof_lines: enzyme from red muscle sarcolemmal membranes

proof_lines: enzyme from white muscle sarcoplasmic reticulum


organism: Oryza sativa


organism: Mesorhizobium loti

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

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

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


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


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


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


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


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

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