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

column_label: Table 1 has separate NADH and NADPH column groups; the export tuple mixes NADH KM with NADPH kcat for the row labeled NADPH.

normalized_value_unit_evidence: For NADPH, KM 7.3 uM = 0.0073 mM; kcat = 3.3 s^-1; kcat/Km = 450 s^-1*mM^-1. The export row uses KM 14.0 mM from the NADH block and kcat 3.3 s^-1 from the NADPH block.

raw_value_unit_evidence: Table 1 wild type row: NADH KM 14 +/- 4.2 mM, NADH kcat 2.2 +/- 0.4 s^-1, NADH kcat/Km 160 M^-1 s^-1; NADPH KM 7.3 +/- 1.0 uM, NADPH kcat 3.3 +/- 0.1 s^-1, NADPH kcat/Km 450 mM^-1 s^-1.

row_label: Wild type; NADPH substrate block

table_label: Table 1, Steady-state kinetic parameters for wild-type and mutant Tfu-FNOs using NADH and NADPH as substrate


organism: Thermobifida fusca

substrate_name: NADPH

source_db: oed

verification_status: unverified

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 R51A with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH

data_origin: experimental

substrate: NADPH

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R51E/R55A with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R51E/R55N with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R51E/R55S with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R51V with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R51V/R55V with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from accession_anchored:Q47RA9 and applied mutation signature R55A to reconstruct the assayed variant sequence.

column_label: PDF page 4, Table 1, R55A row under NADPH columns.

normalized_value_unit_evidence: Km 0.029 mM; kcat 8.8 s^-1; explicit kcat/Km 300 s^-1 mM^-1.

row_label: R55A; NADPH columns

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R55N with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q47RA9 and applied mutation signature R55S to reconstruct the assayed variant sequence.

column_label: PDF page 4, Table 1, R55S row under NADPH Km/kcat/kcat-over-Km columns.

normalized_value_unit_evidence: Km 0.170 mM; kcat 6.9 s^-1; explicit kcat/Km 41 s^-1 mM^-1.

row_label: R55S; NADPH columns


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R55V with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.


enzyme_display_name: FMN reductase [NAD(P)H]

organism: Bacillus subtilis (strain 168)

substrate_name: 4-nitrophenol (NP)(at pH 8 and 25 degrees Celsius)

source_db: uniprot

verification_status: verified

kcat_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

column_label: Table 1; row NP; column Km; raw value 0.2 uM; table abbreviation NP is defined as 4-nitrophenol.

raw_value_unit_evidence: Table 1 NP row, Km column: 0.2 uM.

row_label: NP (4-nitrophenol)

table_label: Table 1: Kinetic Parameters for Nitro-organic Compounds and Chromate

enzyme: FMN reductase [NAD(P)H]

status: verified

source: uniprot


substrate_name: 5-nitro-2-furaldehyde semicarbazone (NF)(at pH 8 and 25 degrees Celsius)

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

column_label: Table 1; row NF; column Km; raw value 0.7 uM. Figure 3A independently states Km = 0.7 uM.

raw_value_unit_evidence: Table 1 NF row, Km column: 0.7 uM.

row_label: NF (nitrofurazone; 5-nitro-2-furaldehyde semicarbazone)


substrate_name: FMN (at pH 8 and 25 degrees Celsius)

assay_conditions_summary: pH 8; 298.15 K; cofactor FMN

column_label: Figure 2A-associated prose; segment external FMN with NADPH; metric Km; raw value 4.2 uM.

raw_value_unit_evidence: Primary prose: reciprocal-FMN replot yields Km = 4.2 uM for FMN.

row_label: External FMN as electron-accepting substrate with NADPH

table_label: Figure 2A-associated primary prose

substrate: FMN (at pH 8 and 25 degrees Celsius)


substrate_name: NADPH (at pH 8 and 25 degrees Celsius)

assay_conditions_summary: pH 8; cofactor NADPH

column_label: The abstract reports Km values for NADPH and NADH of 4.4 microM and 6.4 microM, respectively.

raw_value_unit_evidence: Km raw_value=4.4 microM raw_unit=microM

row_label: Prose segment: NADPH Km

table_label: PubMed PMID 16229462 abstract

substrate: NADPH (at pH 8 and 25 degrees Celsius)


substrate_name: chromate (at pH 8 and 25 degrees Celsius)

column_label: Table 1; row chromate (CrVI); column Km; raw value 5 uM.

raw_value_unit_evidence: Table 1 chromate (CrVI) row, Km column: 5 uM.

row_label: chromate (CrVI)


substrate_name: NADH (at pH 8 and 25 degrees Celsius)

raw_value_unit_evidence: Km raw_value=6.4 microM raw_unit=microM

row_label: Prose segment: NADH Km

substrate: NADH (at pH 8 and 25 degrees Celsius)


substrate_name: methyl-4-nitrobenzenesulfonate (NBS)(at pH 8 and 25 degrees Celsius)

column_label: Table 1; row NBS; column Km; raw value 96 uM. Figure 3B independently states Km = 96 uM.

raw_value_unit_evidence: Table 1 NBS row, Km column: 96 uM.

row_label: NBS


organism: Archaeoglobus fulgidus

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O29370 and applied mutation signature I135A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 295.15 K; cofactor NADPH

column_label: Table 3: NADPH steady-state kinetics parameters for wtFno and I135 variants (Biochemistry and Biophysics Reports 2017); the transcribed row is the body row whose 'Fno' cell reads I135A under the 'Phase 2' block; column 'kcat(s-1)' = 1.24; column 'KmNADPH(uM)' = 2.9; column 'kcat/Km(M-1s-1)' = 4.2 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 1.24 s^-1; already in s^-1, no conversion; the exported value is 1.24 s^(-1). Km: printed cell 2.9 uM; 1 uM is 0.001 mM, so 2.9 / 1000 = 0.0029 mM; the exported value is 0.0029 mM. kcat/Km: printed cell 4.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^5 / 1000 = 420 s^-1 mM^-1, while the export stores 427.58620689655174, the full-precision quotient 1.24 / 0.0029 of the two printed component cells.

raw_value_unit_evidence: Table 3, Phase 2 block, body row I135A: kcat = 1.24 s^-1; KmNADPH = 2.9 uM; printed kcat/Km = 4.2 x 10^5 M^-1 s^-1.

row_label: Table 3 Phase 2 body row whose Fno cell reads I135A, the NADPH steady-state second-phase row for that enzyme form


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O29370 and applied mutation signature I135G to reconstruct the assayed variant sequence.

column_label: Table 3: NADPH steady-state kinetics parameters for wtFno and I135 variants (Biochemistry and Biophysics Reports 2017); the transcribed row is the body row whose 'Fno' cell reads I135G under the 'Phase 2' block; column 'kcat(s-1)' = 0.33; column 'KmNADPH(uM)' = 654; column 'kcat/Km(M-1s-1)' = 5.0 x 10^2.

normalized_value_unit_evidence: kcat: printed cell 0.33 s^-1; already in s^-1, no conversion; the exported value is 0.33 s^(-1). Km: printed cell 654 uM; 1 uM is 0.001 mM, so 654 / 1000 = 0.654 mM; the exported value is 0.654 mM. kcat/Km: printed cell 5.0 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.0 x 10^2 / 1000 = 0.5 s^-1 mM^-1, while the export stores 0.5045871559633027, the full-precision quotient 0.33 / 0.654 of the two printed component cells.

raw_value_unit_evidence: Table 3, Phase 2 block, body row I135G: kcat = 0.33 s^-1; KmNADPH = 654 uM; printed kcat/Km = 5.0 x 10^2 M^-1 s^-1.

row_label: Table 3 Phase 2 body row whose Fno cell reads I135G, the NADPH steady-state second-phase row for that enzyme form


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O29370 and applied mutation signature I135V to reconstruct the assayed variant sequence.

column_label: Table 3: NADPH steady-state kinetics parameters for wtFno and I135 variants (Biochemistry and Biophysics Reports 2017); the transcribed row is the body row whose 'Fno' cell reads I135V under the 'Phase 2' block; column 'kcat(s-1)' = 2.16; column 'KmNADPH(uM)' = 51; column 'kcat/Km(M-1s-1)' = 4.2 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 2.16 s^-1; already in s^-1, no conversion; the exported value is 2.16 s^(-1). Km: printed cell 51 uM; 1 uM is 0.001 mM, so 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed cell 4.2 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.2 x 10^4 / 1000 = 42 s^-1 mM^-1, while the export stores 42.352941176470594, the full-precision quotient 2.16 / 0.051 of the two printed component cells.

raw_value_unit_evidence: Table 3, Phase 2 block, body row I135V: kcat = 2.16 s^-1; KmNADPH = 51 uM; printed kcat/Km = 4.2 x 10^4 M^-1 s^-1.

row_label: Table 3 Phase 2 body row whose Fno cell reads I135V, the NADPH steady-state second-phase row for that enzyme form


substrate_name: oxidized coenzyme F420

column_label: Table 2: FO steady-state kinetics parameters for wtFno and I135 variants (Biochemistry and Biophysics Reports 2017); the transcribed row is the body row whose 'Fno' cell reads I135A; column 'kcat(s-1)' = 1.6; column 'KmFO(uM)' = 3.6; column 'kcat/Km(M-1s-1)' = 4.5 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 1.6 s^-1; already in s^-1, no conversion; the exported value is 1.6 s^(-1). Km: printed cell 3.6 uM; 1 uM is 0.001 mM, so 3.6 / 1000 = 0.0036 mM; the exported value is 0.0036 mM. kcat/Km: printed cell 4.5 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.5 x 10^5 / 1000 = 450 s^-1 mM^-1, while the export stores 444.44444444444446, the full-precision quotient 1.6 / 0.0036 of the two printed component cells.

raw_value_unit_evidence: Table 2, body row I135A: kcat = 1.6 s^-1; KmFO = 3.6 uM; printed kcat/Km = 4.5 x 10^5 M^-1 s^-1.

row_label: Table 2 body row whose Fno cell reads I135A, the FO steady-state row for that enzyme form

substrate: oxidized coenzyme F420


column_label: Table 2: FO steady-state kinetics parameters for wtFno and I135 variants (Biochemistry and Biophysics Reports 2017); the transcribed row is the body row whose 'Fno' cell reads I135G; column 'kcat(s-1)' = 0.7; column 'KmFO(uM)' = 3.6; column 'kcat/Km(M-1s-1)' = 2.0 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 0.7 s^-1; already in s^-1, no conversion; the exported value is 0.7 s^(-1). Km: printed cell 3.6 uM; 1 uM is 0.001 mM, so 3.6 / 1000 = 0.0036 mM; the exported value is 0.0036 mM. kcat/Km: printed cell 2.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.0 x 10^5 / 1000 = 200 s^-1 mM^-1, while the export stores 194.44444444444443, the full-precision quotient 0.7 / 0.0036 of the two printed component cells.

raw_value_unit_evidence: Table 2, body row I135G: kcat = 0.7 s^-1; KmFO = 3.6 uM; printed kcat/Km = 2.0 x 10^5 M^-1 s^-1.

row_label: Table 2 body row whose Fno cell reads I135G, the FO steady-state row for that enzyme form


column_label: Table 2: FO steady-state kinetics parameters for wtFno and I135 variants (Biochemistry and Biophysics Reports 2017); the transcribed row is the body row whose 'Fno' cell reads I135V; column 'kcat(s-1)' = 1.8; column 'KmFO(uM)' = 3.7; column 'kcat/Km(M-1s-1)' = 4.9 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 1.8 s^-1; already in s^-1, no conversion; the exported value is 1.8 s^(-1). Km: printed cell 3.7 uM; 1 uM is 0.001 mM, so 3.7 / 1000 = 0.0037 mM; the exported value is 0.0037 mM. kcat/Km: printed cell 4.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.9 x 10^5 / 1000 = 490 s^-1 mM^-1, while the export stores 486.48648648648646, the full-precision quotient 1.8 / 0.0037 of the two printed component cells.

raw_value_unit_evidence: Table 2, body row I135V: kcat = 1.8 s^-1; KmFO = 3.7 uM; printed kcat/Km = 4.9 x 10^5 M^-1 s^-1.

row_label: Table 2 body row whose Fno cell reads I135V, the FO steady-state row for that enzyme form


enzyme_display_name: FMN reductase (NADPH)

substrate_name: NADPH (with nitrofurazone at pH 7 and at 23 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: NfrA1 FMN nitrofurazone

enzyme: FMN reductase (NADPH)


substrate_name: FMN (with NADPH at pH 7 and at 23 degrees Celsius)

assay_conditions_summary: pH 7; cofactor FMN


substrate_name: nitrofurazone (with NADPH at pH 7 and at 23 degrees Celsius)


organism: Methanogenium organophilum

substrate_name: reduced coenzyme F420

source_db: brenda

sequence: MKVGIMGGTGNIGEGLARRIXIGGKYDVMIKGRDKA

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

substrate: reduced coenzyme F420

source: brenda


sequence_source: multiple

assay_conditions_summary: pH 6; cofactor NADPH

source_databases_merged: brenda uniprot


substrate_name: NADP+

assay_conditions_summary: pH 8; cofactor NADP+

substrate: NADP+


enzyme_display_name: F420-dependent NADP reductase

enzyme: F420-dependent NADP reductase


substrate_name: NADP(+) (at pH 8.0)

substrate: NADP(+) (at pH 8.0)


organism: Escherichia coli

substrate_name: FMN

assay_conditions_summary: pH 7.5; 298.15 K; cofactor FMN

column_label: Table 1 row wild-type SsuE; columns kcat (min^-1), Km (uM), and kcat/Km (uM^-1 min^-1).

normalized_value_unit_evidence: kcat normalized_value=4.25 normalized_unit=s^-1 | km normalized_value=0.00011 normalized_unit=mM | kcat_over_km normalized_value=38333.333333333336 normalized_unit=s^-1 mM^-1

row_label: wild-type SsuE

table_label: Table 1. Steady-State Kinetic Parameters for the Y118 SsuE Variants Measuring NADPH-Dependent FMN Reductase Activity

substrate: FMN


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y118F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Primary FEBS article, PDF page 2 / journal page 125, Results and discussion paragraph beginning with the purified-enzyme properties; the Km sentence explicitly pairs F420, 0.3 mM, and pH 6.0.

raw_value_unit_evidence: The Km values were determined to be 0.3 mM for F420 (pH 6.0).

table_label: Results and discussion kinetic prose, PDF page 2 / journal page 125


substrate_name: NADPH (at pH 6.0)

column_label: Primary FEBS article, PDF page 2 / journal page 125, Results and discussion purified-enzyme paragraph; the Km sentence explicitly pairs NADPH, 50 uM, and pH 6.0.

normalized_value_unit_evidence: Km=0.05 mM after exact conversion of 50 uM.

raw_value_unit_evidence: The Km values were determined to be 50 uM for NADPH (pH 6.0).

row_label: NADPH at pH 6.0

substrate: NADPH (at pH 6.0)


column_label: Primary FEBS article, PDF page 2 / journal page 125, Results and discussion purified-enzyme paragraph; the Km sentence explicitly pairs NADP+, 70 uM, and pH 8.0.

normalized_value_unit_evidence: Km=0.07 mM after exact conversion of 70 uM.

raw_value_unit_evidence: The Km values were determined to be 70 uM for NADP+ (pH 8.0).

row_label: NADP+ at pH 8.0


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADH


substrate_name: NADPH


enzyme_display_name: FMN reductase (NADH)

organism: Pseudomonas putida

substrate_name: FAD

assay_conditions_summary: pH 7.5; 298.15 K; buffer Primary measurement evidence: evidence location type: prose; cofactor FAD

column_label: Journal page 3287, Results prose subsection Substrate specificity and kinetic properties of Fred (there is no kinetic table for Fred in this paper). The sentence reports two flavin measurements: for FMN the printed values are Km 3.6 uM, kcat 283 s^-1 and kcat/Km 7.9 x 10^7; for FAD they are Km 19 uM, kcat 128 s^-1 and kcat/Km 6.7 x 10^6. The measurement read for this record is the FAD one: printed Km 19 uM, printed kcat 128 s^-1 and printed kcat/Km 6.7 x 10^6.

normalized_value_unit_evidence: kcat: printed 128 s^-1; the value is already in s^-1, so no unit conversion applies; the catalog value is 128.0 s^(-1). Km: printed 19 uM; 19 / 1000 = 0.019 mM; the catalog value is 0.019 mM. kcat/Km: the catalog value 6736.842105263158 s^(-1)*mM^(-1) is the full-precision quotient 128 / 0.019 of those same two printed cells. The paper additionally prints its own kcat/Km numeral 6.7 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so that numeral converts to 6700.0 s^-1 mM^-1, and the full-precision quotient rounds to the same two significant digits the paper prints, so the printed numeral corroborates the catalog quotient and no metric changes.

raw_value_unit_evidence: Reviewed tuple for FAD. The reviewed primary measurement is stated in the Results subsection Substrate specificity and kinetic properties of Fred, journal page 3287. The matched measurement is FAD reduction by purified Fred. The measured construct is purified Fred flavin reductase of Pseudomonas putida ATCC 17453. The measured substrate is FAD, the flavin whose reduction by Fred was assayed. The assay condition is pH 7.5, 25 C, 50 mM Tris-HCl buffer. Fred with FAD as the varied substrate: kcat 128 s^-1. Fred with FAD as the varied substrate: Km 19 uM. Fred with FAD as the varied substrate: printed kcat/Km 6.7 x 10^6 M^-1 s^-1, where the numeral is printed in the paper and the unit is resolved from the printed components.

row_label: FAD reduction by purified Fred

table_label: No table: the values are printed in the Results prose on journal page 3287

enzyme: FMN reductase (NADH)

substrate: FAD


enzyme_display_name: carboxynorspermidine synthase

organism: Vibrio alginolyticus

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Abstract reports the Km value for NADPH was 1.51 mM.

raw_value_unit_evidence: Km raw_value=1.51 mM raw_unit=mM

row_label: Vibrio alginolyticus carboxynorspermidine synthase / NADPH

table_label: PubMed XML abstract PMID 1955861

enzyme: carboxynorspermidine synthase


organism: Sulfitobacter sp.

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


organism: Bacillus cereus

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

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH


organism: Vibrio harveyi

assay_conditions_summary: pH 7; 296.15 K; cofactor NADPH


enzyme_display_name: 2-methyl-1-pyrroline reductase

organism: Streptomyces sp.

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

enzyme: 2-methyl-1-pyrroline reductase


organism: Hyphomicrobium nitrativorans

substrate_name: dihydrosarcinapterin

substrate: dihydrosarcinapterin


organism: Paracoccus denitrificans

sequence: SRLPPATRDKLADEITFFPA

wild_type_sequence: SRLPPATRDKLADEITFFPA

assay_conditions_summary: pH 7.4; 303.15 K; buffer 25 mM Tris/HCl; cofactor NADH

column_label: Official Wiley PDF text extract, printed page 560, Table 3: columns Substrate (variable concentration), Second substrate (fixed concentrations), Third substrate, and Km (uM); accompanying caption gives kcat values for FerA Fe(III) reductase and FMN reductase activities.

normalized_value_unit_evidence: For the queued NADH substrate, the printed NADH Km normalizes to 0.011 mM, not 0.02 mM. The exported 0.02 mM Km corresponds to the FMN row, and 28 / 0.020 = 1400 s^-1 mM^-1 is a derived FMN ratio rather than a primary NADH kcat/Km cell.

raw_value_unit_evidence: Table 3 reports FerA FMN reductase kinetic parameters: variable NADH with FMN as second substrate has Km 11 +/- 5 uM; variable FMN with NADH as second substrate has Km 20 +/- 8 uM. The text states kcat is 28 +/- 6 s^-1 for FerA FMN reductase activity. No kcat/Km column is printed.

row_label: FerA, FMN reductase activity

table_label: Table 3


organism: Methylobacterium nodulans


organism: Paenibacillus lactis

km_display: Not reported


organism: Streptomyces sp. GF3587

assay_conditions_summary: cofactor NADPH

column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5e (R = cyclohexyl); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 5e (R = cyclohexyl) reports Vmax 0.0388; kcat 0.0215 s^-1; Km 1.55 mM; kcat/Km 0.0139 s^-1 mM^-1.

row_label: Table 3 row 5e (R = cyclohexyl); 6-cyclohexyl-2,3,4,5-tetrahydropyridine


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5j (R = isopropenyl); columns kcat.

raw_value_unit_evidence: Table 3 row 5j (R = isopropenyl) reports Vmax 4.24; kcat 2.35 s^-1.

row_label: Table 3 row 5j (R = isopropenyl); 6-(prop-1-en-2-yl)-2,3,4,5-tetrahydropyridine


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5l (R = 2-thienyl); columns Km.

raw_value_unit_evidence: Table 3 row 5l (R = 2-thienyl) reports Vmax 1.16; Km 0.244 mM.

row_label: Table 3 row 5l (R = 2-thienyl); 6-(thiophen-2-yl)-2,3,4,5-tetrahydropyridine


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 7a (R = Me); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 7a (R = Me) reports Vmax 0.340; kcat 0.189 s^-1; Km 0.155 mM; kcat/Km 1.22 s^-1 mM^-1.

row_label: Table 3 row 7a (R = Me); 1-methyl-3,4-dihydroisoquinoline


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5c (R = p-MeOPh); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 5c (R = p-MeOPh) reports Vmax 0.474; kcat 0.263 s^-1; Km 1.05 mM; kcat/Km 0.250 s^-1 mM^-1.

row_label: Table 3 row 5c (R = p-MeOPh); 6-(4-methoxyphenyl)-2,3,4,5-tetrahydropyridine


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 1a (R = Me); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 1a (R = Me) reports Vmax 0.633; kcat 0.351 s^-1; Km 1.88 mM; kcat/Km 0.187 s^-1 mM^-1.

row_label: Table 3 row 1a (R = Me); 2-methyl-1-pyrroline


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 9 (R = H); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 9 (R = H) reports Vmax 1.905; kcat 1.057 s^-1; Km 0.481 mM; kcat/Km 2.195 s^-1 mM^-1.

row_label: Table 3 row 9 (R = H); 2-methyl-3,4-dihydroisoquinolin-2-ium


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


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5a (R = Me); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 5a (R = Me) reports Vmax 7.60; kcat 4.21 s^-1; Km 0.371 mM; kcat/Km 11.4 s^-1 mM^-1.

row_label: Table 3 row 5a (R = Me); 6-methyl-2,3,4,5-tetrahydropyridine


column_label: Table 3. Kinetics data for cyclic imine substrates 1-7; row 5i (R = n-propyl); columns kcat, Km, kcat/Km.

raw_value_unit_evidence: Table 3 row 5i (R = n-propyl) reports Vmax 8.35; kcat 4.63 s^-1; Km 0.804 mM; kcat/Km 5.76 s^-1 mM^-1.

row_label: Table 3 row 5i (R = n-propyl); 6-propyl-2,3,4,5-tetrahydropyridine


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.2; cofactor NADPH

proof_lines: wild-type, cosubstrate NADPH, pH 7.2, temperature not specified in the publication


proof_lines: wild-type, pH 7.2, temperature not specified in the publication


proof_lines: Chimera-1, cosubstrate NADPH, pH 7.2, temperature not specified in the publication

proof_lines: Chimera-1, cosubstrate NADH, pH 7.2, temperature not specified in the publication


enzyme_display_name: staphylopine dehydrogenase

organism: Staphylococcus aureus

substrate_name: glyoxylate

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

assay_conditions_summary: pH 8; 295.15 K; buffer 50 mM Tris pH 8; cofactor NADPH

column_label: Table 1 row SaODH Glyoxylate NADPH d-HisNA; columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row SaODH Glyoxylate NADPH d-HisNA: kcat=0.074 +/- 0.003 s^-1; Km=3000 +/- 200 uM; kcat/Km=24 +/- 2 M^-1 s^-1.

row_label: SaODH / Glyoxylate / NADPH / d-HisNA

table_label: Table 1

source_databases_merged: brenda skid uniprot

enzyme: staphylopine dehydrogenase

substrate: glyoxylate


substrate_name: pyruvate

column_label: Table 1 row SaODH Pyruvate NADPH d-HisNA; columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row SaODH Pyruvate NADPH d-HisNA: kcat=0.26 +/- 0.01 s^-1; Km=29 +/- 2 uM; kcat/Km=8900 +/- 700 M^-1 s^-1.

row_label: SaODH / Pyruvate / NADPH / d-HisNA

substrate: pyruvate


substrate_name: oxaloacetate

column_label: Table 1 row SaODH Oxaloacetate NADPH d-HisNA; columns kcat (s^-1), Km (uM), and kcat/Km (M^-1 s^-1).

raw_value_unit_evidence: Table 1 row SaODH Oxaloacetate NADPH d-HisNA: kcat=0.26 +/- 0.01 s^-1; Km=1400 +/- 100 uM; kcat/Km=180 +/- 10 M^-1 s^-1.

row_label: SaODH / Oxaloacetate / NADPH / d-HisNA

substrate: oxaloacetate


organism: Homo sapiens


organism: Colwellia psychrerythraea

substrate_name: L-proline

assay_conditions_summary: pH 10.5; cofactor NADP+

proof_lines:
pH 10.5, 30°C, cosubstrate: NAD+
pH 10.5, 30°C, cosubstrate: NADP+

substrate: L-proline


assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines:
pH 6.5, 30°C, cosubstrate: NADH
pH 6.5, 30°C, cosubstrate: NADPH


organism: Ancylobacter novellus (strain ATCC 8093 / DSM 506 / JCM 20403 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIMB 10456)

proof_lines: kcat is 26 sec(-1) for Pyr2C reduction using NADPH.


organism: Shewanella loihica

substrate_name: 1-Pyrroline-2-carboxylate; H+; NADPH

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

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

substrate: 1-Pyrroline-2-carboxylate; H+; NADPH


organism: Silicibacter pomeroyi

substrate_name: H+; NADPH; 1-Pyrroline-2-carboxylate

substrate: H+; NADPH; 1-Pyrroline-2-carboxylate


substrate_name: D-Histidine nicotianamine; H+; NADPH; Pyruvate


organism: Burkholderia pseudomallei


organism: Burkholderia thailandensis

substrate_name: H+; 1-Pyrroline-2-carboxylate; NADPH

substrate: H+; 1-Pyrroline-2-carboxylate; NADPH


substrate_name: NADPH; 1-Pyrroline-2-carboxylate; H+

substrate: NADPH; 1-Pyrroline-2-carboxylate; H+


organism: Pseudomonas aeruginosa


organism: Rhodobacter sphaeroides


organism: Roseobacter denitrificans


organism: Methylorubrum extorquens

assay_conditions_summary: pH 5.3; cofactor NADPH

column_label: Article Table 2 row M. extorquens AM1 DmrA-H4 columns KM(app)=193 +/- 71 uM and kcat(s^-1)=1.5; kcat/Km is calculated from those same-row cells.

raw_value_unit_evidence: Table 2 row reports KM(app) 193 +/- 71 uM and kcat 1.5 s^-1 for M. extorquens AM1 DmrA-H4; prose identifies 193 uM H2SPT.

row_label: M. extorquens AM1 DmrA-H4

table_label: Table 2


proof_lines: pH 5.3, temperature not specified in the publication


organism: Agrobacterium tumefaciens

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

proof_lines: kcat is 32 sec(-1) for Pyr2C reduction using NADPH.


organism: Bacillus cereus

proof_lines: kcat is 5.8 sec(-1) for Pyr2C reduction using NADPH. kcat is 0.87 sec(-1) for Pyr2C reduction using NADH.


proof_lines: kcat is 15 sec(-1) for Pyr2C reduction using NADPH. kcat is 19 sec(-1) for Pyr2C reduction using NADH.


substrate_name: NADPH; H+; 1-Pyrroline-2-carboxylate

proof_lines: kcat is 15 sec(-1) for Pyr2C reduction using NADPH. kcat is 2.1 sec(-1) for Pyr2C reduction using NADH.

substrate: NADPH; H+; 1-Pyrroline-2-carboxylate


organism: Bacillus thuringiensis

proof_lines: kcat is 11 sec(-1) for Pyr2C reduction using NADPH. kcat is 2.1 sec(-1) for Pyr2C reduction using NADH.


organism: Pseudomonas fluorescens


proof_lines: kcat is 20 sec(-1) for Pyr2C reduction using NADPH.


enzyme_display_name: Dihydromonapterin reductase

organism: Escherichia coli (strain K12)

substrate_name: Unknown

enzyme: Dihydromonapterin reductase

substrate: Unknown


organism: Staphylococcus aureus

assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH

column_label: Table 1 row SaODH NADPH; alpha-keto acid Pyruvate; HisNA substrate d-HisNA; column kcat (s^-1).

raw_value_unit_evidence: Table 1 row SaODH NADPH with Pyruvate and d-HisNA: kcat=0.26 +/- 0.01 s^-1.

row_label: SaODH / NADPH / Pyruvate / d-HisNA

source_databases_merged: brenda skid

substrate: NADPH


smiles: O=CC(=O)O


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


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


organism: Burkholderia ambifaria

proof_lines: kcat is 106 sec(-1) for Pyr2C reduction using NADPH. kcat is 41 sec(-1) for Pyr2C reduction using NADH.


substrate_name: 1-Pyrroline-2-carboxylate; NADPH; H+

proof_lines: kcat is 54 sec(-1) for Pyr2C reduction using NADPH.

substrate: 1-Pyrroline-2-carboxylate; NADPH; H+


organism: Burkholderia multivorans

proof_lines: kcat is 33 sec(-1) for Pyr2C reduction using NADPH.


proof_lines: kcat is 25 sec(-1) for Pyr2C reduction using NADPH.


organism: Colwellia psychrerythraea (strain 34H / ATCC BAA-681)

substrate_name: Delta(1)-pyrroline-2-carboxylate (using NADPH, at pH 6.5)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature H2C with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: kcat is 7470 min(-1) for Pyr2C reduction using NADPH. kcat is 621 min(-1) for Pyr2C reduction using NADH. kcat is 82.0 min(-1) for Pip2C reduction using NADPH. kcat is 5.27 min(-1) for Pip2C reduction using NADH. kcat is 61.3 min(-1) for De


organism: Paracoccus denitrificans

proof_lines: kcat is 260 sec(-1) for Pyr2C reduction using NADPH. kcat is 81 sec(-1) for Pyr2C reduction using NADH.


assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADPH

column_label: Table 7 (PDF page 17 of 32); OCD_PRS_navy (5); row group `Q63FA5 | BCE33L0803`; Cofactor sub-row `NADH`; columns kcat [s-1] = `0.87`, KM [mM] = `4.9`, kcat/KM[M-1s-1] = `180`.

normalized_value_unit_evidence: kcat: printed cell 0.87 s^-1 -> 0.87 s^(-1); the export holds 0.87 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 4.9 mM -> 4.9 mM; the export holds 4.9 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 180 M^-1 s^-1 converted as 180 / 1000 = 0.18 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 0.17755102040816326 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 7, row group `Q63FA5 | BCE33L0803`, sub-row `NADH`: kcat = 0.87 s^-1; KM = 4.9 mM; kcat/KM = 180 M^-1 s^-1.

row_label: Q63FA5 | BCE33L0803 / NADH (Table 7 OCD_PRS_navy (5))

table_label: Table 7. Kinetic constants for the proline ketimine reductases (members of the malate/Llactate dehydrogenase 2 [MLD2] and ornithine cyclodeaminase [OCD] superfamilies) that are in the genome neighborhoods of members of the PRS


proof_lines:
PRS family
Bacillus cereus
1-Pyrroline-2-carboxylate


organism: Colwellia psychrerythraea

assay_conditions_summary: pH 6.5; 303.15 K; buffer 50 mM potassium phosphate; cofactor NADPH

column_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. Row CpLhpI (Colwellia psychrerythraea) | Pyr2C | NADPH; pH cell 6.5; column 'K m (mM)' = 5.90 ± 0.36; column 'k cat (min^-1)' = 7470 ± 470; column 'k cat / K m (min^-1 mM^-1)' = 1270 ± 2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7470 ± 470 min^-1; 7470 / 60 = 124.5 s^(-1) exactly; the exported value is 124.5 s^(-1) and already agrees. Km: printed Table 1 cell 5.90 ± 0.36 mM; the paper prints Km in mM already, so the value stands at 5.9 mM; the exported value is 1.8 mM. kcat/Km: printed Table 1 cell 1270 ± 2 min^-1 mM^-1; 1270 / 60 = 21.166666666666668 s^-1 mM^-1; the exported value is 69.16666666666667 s^(-1)*mM^(-1), which is the bare quotient 124.5 / 1.8 of the export's own two stored numbers.

raw_value_unit_evidence: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. | metric header row of the table: Enzymes Substrates pH a Coenzymes Specific activity (units/mg protein) K m (mM) k cat (min −1 ) k cat / K m b (min −1 mM −1 ) | row CpLhpI (Colwellia psychrerythraea) | Pyr2C | NADPH cells read: specific activity 30.2 units/mg protein, K m = 5.90 ± 0.36 mM, k cat = 7470 ± 470 min^-1, k cat / K m = 1270 ± 2 min^-1 mM^-1.

row_label: Table 1, row CpLhpI (Colwellia psychrerythraea) | Pyr2C | NADPH


column_label: Table label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. Row: CpLhpI | Pip2C. Coenzyme: NADPH. Columns read: K m (mM) cell 7.26 ± 1.22, k cat (min^-1) cell 82.9 ± 13.7, k cat / K m (min^-1 mM^-1) cell 11.4 ± 0.2. metric: kcat; raw value: 82.9 ± 13.7; raw unit: min^-1; normalized value: 1.382 s^(-1); metric: Km; raw value: 7.26 ± 1.22; raw unit: mM; normalized value: 7.26 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.19035812672176308 s^-1 mM^-1; assay condition: All enzyme assays were performed at 30 C. Pyr2C/Pip2C reductase was assayed routinely in the direction of Pyr2C reduction by measuring the oxidization of NAD(P)H at 340 nm; the standard assay mixture contained 10 mM Pyr2C (or Pip2C) in 50 mM potassium phosphate buffer, pH 6.5 for AbLhpI and CpLhpI; the reactions were started by the addition of 100 uL of a 1.5 mM NAD(P)H solution to a final volume of 1 mL; K m and k cat values were calculated by a Lineweaver-Burk plot. Export row conditions: pH 6.5.

normalized_value_unit_evidence: CpLhpI | Pip2C | NADPH row of Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. K m 7.26 ± 1.22 mM = 7.26 mM (the paper already prints K m in mM, so no conversion is needed); k cat 82.9 ± 13.7 min^-1 = 82.9 / 60 = 1.3816666666666668 s^-1 (1 min^-1 = 1/60 s^-1), which is 1.382 s^-1 at the export's stored precision; k cat / K m 1.382 s^-1 / 7.26 mM = 0.19035812672176308 s^-1 mM^-1. The paper's own printed k cat / K m cell 11.4 ± 0.2 min^-1 mM^-1 = 11.4 / 60 s^-1 mM^-1 agrees with that quotient at the printed cell's own precision. In the table asset the superscript minus one renders as the U+2212 sign in the headers `k cat (min −1 )` and `k cat / K m b (min −1 mM −1 )`, subscripts are flattened so K m and k cat print with a space, the substrate names print as `Pyr4 S H2C`, `Pip2C` and `l -Pipecolate`, and each cell carries its standard deviation after the ± sign.

raw_value_unit_evidence: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction. | metric header row of the table: Enzymes Substrates pH a Coenzymes Specific activity (units/mg protein) K m (mM) k cat (min −1 ) k cat / K m b (min −1 mM −1 ) | row: Pip2C NADPH 0.291 7.26 ± 1.22 82.9 ± 13.7 11.4 ± 0.2 | CpLhpI | Pip2C | NADPH cells read: specific activity, then K m = 7.26 ± 1.22 mM, k cat = 82.9 ± 13.7 min^-1, k cat / K m = 11.4 ± 0.2 min^-1 mM^-1.

row_label: CpLhpI | Pip2C


mutation_signature: Δ1

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Δ1 to reconstruct the assayed variant sequence.

mutation_type: deletion

assay_conditions_summary: pH 6.5; 303.15 K; buffer 10 mM Pyr2C or Pip2C in 50 mM potassium phosphate; cofactor NADPH

column_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction; row CpLhpI / Pyr2C / NADPH; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 5.90 ± 0.36 mM | kcat 7470 ± 470 min^-1 | kcat/Km 1270 ± 2 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=124.5 normalized_unit=s^-1; Km normalized_value=5.9 normalized_unit=mM; kcat/Km normalized_value=21.101694915254235 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7470 ± 470 raw_unit=min^-1; Km raw_value=5.90 ± 0.36 raw_unit=mM; kcat/Km raw_value=1270 ± 2 raw_unit=min^-1*mM^-1

row_label: CpLhpI / Pyr2C / NADPH


substrate_name: L-Pipecolate

column_label: Table label: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction. Row: CpLhpI | l -Pipecolate. Coenzyme: NADP +. Columns read: K m (mM) cell 80.1 ± 2.8, k cat (min^-1) cell 1.28 ± 0.04, k cat / K m (min^-1 mM^-1) cell 0.016 ± 0.001. metric: kcat; raw value: 1.28 ± 0.04; raw unit: min^-1; normalized value: 0.021 s^(-1); metric: Km; raw value: 80.1 ± 2.8; raw unit: mM; normalized value: 80.1 mM; metric: kcat/Km; raw value: 0.016 ± 0.001; raw unit: min^-1 mM^-1; normalized value: 0.0002666666666666667 s^-1 mM^-1; explicit printed primary cell; assay condition: All enzyme assays were performed at 30 C. To assay the reverse reaction, the reaction mixture consisted of 50 mM Glycine-NaOH buffer, pH 10.5 for AbLhpI and CpLhpI, and 10 mM l -proline (or l -pipecolate); the reaction was started by the addition of 15 mM NAD(P) + (100 uL) with a final reaction volume of 1 mL; K m and k cat values were calculated by a Lineweaver-Burk plot. Export row conditions: pH 10.5.

normalized_value_unit_evidence: kcat raw 1.28 ± 0.04 min^-1 -> 0.021 s^(-1); Km raw 80.1 ± 2.8 mM -> 80.1 mM; explicit printed kcat/Km raw 0.016 ± 0.001 min^-1 mM^-1 -> 0.0002666666666666667 s^-1 mM^-1. Conversion: 0.016 min^-1 mM^-1 / 60 = 1/3750 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction. | metric header row of the table: Enzymes Substrates pH a Coenzymes Specific activity (units/mg protein) K m (mM) k cat (min −1 ) k cat / K m b (min −1 mM −1 ) | row: l -Pipecolate NADP + 0.00435 80.1 ± 2.8 1.28 ± 0.04 0.016 ± 0.001 | CpLhpI | l -Pipecolate | NADP + cells read: specific activity, then K m = 80.1 ± 2.8 mM, k cat = 1.28 ± 0.04 min^-1, k cat / K m = 0.016 ± 0.001 min^-1 mM^-1.

row_label: CpLhpI | l -Pipecolate

substrate: L-Pipecolate


substrate_name: L-Proline

substrate: L-Proline


enzyme_display_name: dihydromonapterin reductase

assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH

column_label: Table 1. Summary of kinetic parameters and substrate specificities for PruA from A. tumefaciens compared to homologs from B. abortus and P. aeruginosa; row P. aeruginosa PA3437 / H2BPt; columns kcat s^-1 raw 0.8, Km uM raw 75.7 +/- 13.5, kcat/Km M^-1*s^-1 raw 1.1 x 10^4; normalized paper kcat 0.8 s^-1, Km 0.0757 mM, same-row kcat/Km 10.568031704095114 s^-1*mM^-1; export values kcat 0.8 s^-1, Km 0.757 mM, kcat/Km 1.0568031704095113 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.8 normalized_unit=s^-1; Km normalized_value=0.0757 normalized_unit=mM from 75.7 +/- 13.5 uM / 1000; kcat/Km normalized_value=10.568031704095114 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1.1 x 10^4 M^-1*s^-1

raw_value_unit_evidence: kcat raw_value=0.8 raw_unit=s^-1; Km raw_value=75.7 +/- 13.5 raw_unit=uM; kcat/Km raw_value=1.1 x 10^4 raw_unit=M^-1*s^-1

row_label: P. aeruginosa PA3437 / H2BPt

enzyme: dihydromonapterin reductase


column_label: Table 1. Summary of kinetic parameters and substrate specificities for PruA from A. tumefaciens compared to homologs from B. abortus and P. aeruginosa; row P. aeruginosa PA3437 / H2MPt; columns kcat s^-1 raw 1.9, Km uM raw 170.0 +/- 31.2, kcat/Km M^-1*s^-1 raw 1.1 x 10^4; normalized paper kcat 1.9 s^-1, Km 0.17 mM, same-row kcat/Km 11.176470588235293 s^-1*mM^-1; export values kcat 1.9 s^-1, Km 0.17 mM, kcat/Km 11.176470588235293 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=1.9 normalized_unit=s^-1; Km normalized_value=0.17 normalized_unit=mM from 170.0 +/- 31.2 uM / 1000; kcat/Km normalized_value=11.176470588235293 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=1.1 x 10^4 M^-1*s^-1

raw_value_unit_evidence: kcat raw_value=1.9 raw_unit=s^-1; Km raw_value=170.0 +/- 31.2 raw_unit=uM; kcat/Km raw_value=1.1 x 10^4 raw_unit=M^-1*s^-1

row_label: P. aeruginosa PA3437 / H2MPt


column_label: Table 1. Summary of kinetic parameters and substrate specificities for PruA from A. tumefaciens compared to homologs from B. abortus and P. aeruginosa; row P. aeruginosa PA3437 / H2NPt; columns kcat s^-1 raw 0.7, Km uM raw 90.0 +/- 20.3, kcat/Km M^-1*s^-1 raw 7.8 x 10^3; normalized paper kcat 0.7 s^-1, Km 0.09 mM, same-row kcat/Km 7.777777777777778 s^-1*mM^-1; export values kcat 0.7 s^-1, Km 0.9 mM, kcat/Km 0.7777777777777777 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.7 normalized_unit=s^-1; Km normalized_value=0.09 normalized_unit=mM from 90.0 +/- 20.3 uM / 1000; kcat/Km normalized_value=7.777777777777778 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=7.8 x 10^3 M^-1*s^-1

raw_value_unit_evidence: kcat raw_value=0.7 raw_unit=s^-1; Km raw_value=90.0 +/- 20.3 raw_unit=uM; kcat/Km raw_value=7.8 x 10^3 raw_unit=M^-1*s^-1

row_label: P. aeruginosa PA3437 / H2NPt


column_label: Official eLife HTML Table 7 row Q0B9S2 / Bamb_3547 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=54 normalized_unit=s^-1; Km normalized_value=9.4 normalized_unit=mM; kcat/KM normalized_value=5.7 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=54 +/- 13 raw_unit=s^-1; Km raw_value=9.4 +/- 4 raw_unit=mM; kcat/KM raw_value=5700 raw_unit=M^-1 s^-1

row_label: Q0B9S2 / Bamb_3547 / NADPH

table_label: Table 7. Kinetic constants for the proline ketimine reductases


column_label: Official eLife HTML Table 7 row A9AKH1 / Bmul_4263 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=25 normalized_unit=s^-1; Km normalized_value=4 normalized_unit=mM; kcat/KM normalized_value=6.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=25 +/- 6 raw_unit=s^-1; Km raw_value=4 +/- 2 raw_unit=mM; kcat/KM raw_value=6400 raw_unit=M^-1 s^-1

row_label: A9AKH1 / Bmul_4263 / NADPH


column_label: Official eLife HTML Table 7 row A9ALD3 / Bmul_4451 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=33 normalized_unit=s^-1; Km normalized_value=7.4 normalized_unit=mM; kcat/KM normalized_value=4.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=33 +/- 2 raw_unit=s^-1; Km raw_value=7.4 +/- 1 raw_unit=mM; kcat/KM raw_value=4400 raw_unit=M^-1 s^-1

row_label: A9ALD3 / Bmul_4451 / NADPH


substrate_name: 7,8-dihydrofolate (at pH 6.0)

assay_conditions_summary: pH 6

proof_lines: FolM, A New Chromosomally Encoded Dihydrofolate Reductase in Escherichia coli

substrate: 7,8-dihydrofolate (at pH 6.0)


substrate_name: NADPH (at pH 6.0)

assay_conditions_summary: pH 6; cofactor NADPH

substrate: NADPH (at pH 6.0)


substrate_name: NADPH

assay_conditions_summary: pH 7.5; cofactor NADPH


column_label: Official eLife HTML Table 7 row Q7CVK1 / Atu4676 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=32 normalized_unit=s^-1; Km normalized_value=0.33 normalized_unit=mM; kcat/KM normalized_value=99 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=32 +/- 1 raw_unit=s^-1; Km raw_value=0.33 +/- 0.04 raw_unit=mM; kcat/KM raw_value=99000 raw_unit=M^-1 s^-1

row_label: Q7CVK1 / Atu4676 / NADPH


assay_conditions_summary: pH 5.3; 296.15 K; cofactor NADPH


organism: Burkholderia pseudomallei

proof_lines:
PRS family
Bacillus cereus


column_label: Table 7 (PDF page 17 of 32); MLD2_PRS_light skyblue (3); row group `Q9I492 | PA1252`; Cofactor sub-row `NADPH`; columns kcat [s-1] = `1.6`, KM [mM] = `0.41`, kcat/KM[M-1s-1] = `3900`.

normalized_value_unit_evidence: kcat: printed cell 1.6 s^-1 -> 1.6 s^(-1); the export holds 1.6 s^(-1); no unit conversion applied (the paper's kcat column is already s^-1). Km: printed cell 0.41 mM -> 0.41 mM; the export holds 0.41 mM; no unit conversion applied (the paper's KM column is already mM). kcat/Km: printed cell 3900 M^-1 s^-1 converted as 3900 / 1000 = 3.9 s^-1 mM^-1 (M^-1 s^-1 / 1000 = s^-1 mM^-1); the export holds 3.9024390243902443 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 7, row group `Q9I492 | PA1252`, sub-row `NADPH`: kcat = 1.6 s^-1; KM = 0.41 mM; kcat/KM = 3900 M^-1 s^-1.

row_label: Q9I492 | PA1252 / NADPH (Table 7 MLD2_PRS_light skyblue (3))


organism: Burkholderia thailandensis


column_label: Official eLife HTML Table 7 row Q3IZJ8 / RSP_0854 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=66 normalized_unit=s^-1; Km normalized_value=0.43 normalized_unit=mM; kcat/KM normalized_value=150 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=66 +/- 4 raw_unit=s^-1; Km raw_value=0.43 +/- 0.09 raw_unit=mM; kcat/KM raw_value=150000 raw_unit=M^-1 s^-1

row_label: Q3IZJ8 / RSP_0854 / NADPH


column_label: Official eLife HTML Table 7 row Q4KGT8 / PFL_1416 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=20 normalized_unit=s^-1; Km normalized_value=1.1 normalized_unit=mM; kcat/KM normalized_value=18 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=20 +/- 0.8 raw_unit=s^-1; Km raw_value=1.1 +/- 0.2 raw_unit=mM; kcat/KM raw_value=18000 raw_unit=M^-1 s^-1

row_label: Q4KGT8 / PFL_1416 / NADPH


organism: Shewanella loihica


substrate_name: 7,8-dihydromonapterin (at pH 6.0)

substrate: 7,8-dihydromonapterin (at pH 6.0)


organism: Silicibacter pomeroyi

column_label: Official eLife HTML Table 7 row Q5LLV0 / SPO3821 / NADPH; columns kcat [s^-1], Km [mM], and kcat/KM [M^-1 s^-1]; DOI table https://doi.org/10.7554/eLife.03275.015

normalized_value_unit_evidence: kcat normalized_value=130 normalized_unit=s^-1; Km normalized_value=3.0 normalized_unit=mM; kcat/KM normalized_value=43 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=130 +/- 20 raw_unit=s^-1; Km raw_value=3.0 +/- 0.9 raw_unit=mM; kcat/KM raw_value=43000 raw_unit=M^-1 s^-1

row_label: Q5LLV0 / SPO3821 / NADPH


organism: Escherichia coli

substrate_name: FMN

assay_conditions_summary: pH 7.9; 303.15 K; cofactor FMN

substrate: FMN


substrate_name: FAD

assay_conditions_summary: pH 7.9; 303.15 K; cofactor FAD

substrate: FAD


assay_conditions_summary: pH 7.9; 303.15 K; cofactor NADPH


substrate_name: NADH

assay_conditions_summary: pH 7.9; 303.15 K; cofactor NADH

substrate: NADH


organism: Homo sapiens

proof_lines: wild-type, pH 6.6, temperature not specified in the publication


mutation_signature: truncated protein

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

mutation_type: truncation

proof_lines: truncated protein, residues 38-644, pH 6.6, temperature not specified in the publication


assay_conditions_summary: pH 6.6; cofactor NADPH


assay_conditions_summary: pH 6.6; cofactor NADH


ki_unit: mM


organism: Pseudomonas putida

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


enzyme_display_name: glutamate dehydrogenase (NADP+)

substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25°C

enzyme: glutamate dehydrogenase (NADP+)

substrate: NADP+


proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 1960 micromol/min/mg, pH 8.0, 25°C


substrate_name: L-glutamate

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

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25°C

substrate: L-glutamate


enzyme_display_name: UniProt B9L163

organism: Thermomicrobium roseum

substrate_name: N-Methyl-L-alanine

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt B9L163

substrate: N-Methyl-L-alanine

source: skid


substrate_name: N-methyl-L-phenylalanine

substrate: N-methyl-L-phenylalanine


substrate_name: N-methyl-L-tryptophan

substrate: N-methyl-L-tryptophan


substrate_name: L-proline

substrate: L-proline


substrate_name: N-methyl-D-proline

substrate: N-methyl-D-proline


substrate_name: N-methyl-L-aspartate

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

substrate: N-methyl-L-aspartate


substrate_name: N-Methyl-L-leucine

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

substrate: N-Methyl-L-leucine


enzyme_display_name: UniProt P40859

organism: Bacillus sp. (in: Bacteria)

substrate_name: sarcosine

smiles: CNCC(=O)O

enzyme: UniProt P40859

substrate: sarcosine


enzyme_display_name: alanine dehydrogenase

organism: Halobacterium salinarum

assay_conditions_summary: cofactor NADH

enzyme: alanine dehydrogenase


substrate_name: L-Ala

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

substrate: L-Ala


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

assay_conditions_summary: pH 8; buffer 50 mM triethanolamine; cofactor NADP+

proof_lines: mutant enzyme R443S/G456A, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP

enzyme: glutamate dehydrogenase [NAD(P)+]


smiles: N


organism: Paenarthrobacter ureafaciens

substrate_name: N-Methyl-DL-alanine

substrate: N-Methyl-DL-alanine


enzyme_display_name: N6-methyl-lysine oxidase

organism: Rattus norvegicus

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

enzyme: N6-methyl-lysine oxidase


organism: Mycolicibacterium smegmatis


assay_conditions_summary: pH 7.2; 296.15 K; cofactor NADH


organism: Achromobacter denitrificans


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

proof_lines:
crude extract
partially purified enzyme


enzyme_display_name: N-methyl-L-amino-acid oxidase

organism: Oryctolagus cuniculus

substrate_name: alpha-N-methyl-L-tryptophan

enzyme: N-methyl-L-amino-acid oxidase

substrate: alpha-N-methyl-L-tryptophan


organism: Bacillus sp. (in: firmicutes)

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K265Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


sequence_variant_note: Mutation signature K265A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K265M could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature K265R could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Synechocystis sp. PCC 6803

smiles: C(CN)CN

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines: at pH 7.4, temperature not specified in the publication

proof_lines: kcat is 2.57 sec(-1) with agmatine as substrate. kcat is 0.32 sec(-1) with putrescine as substrate. kcat is 0.07 sec(-1) with 1,3-diaminopropane as substrate. kcat is 2.43 sec(-1) with NADPH as substrate.


substrate_name: putrescine

smiles: C(CCN)CN

substrate: putrescine


substrate_name: agmatine

smiles: C(CCN=C(N)N)CN

proof_lines: with NADPH as cosubstrate, at pH 7.4, temperature not specified in the publication

substrate: agmatine


substrate_name: NADPH

substrate: NADPH


substrate_name: NADH

substrate: NADH


organism: Arthrobacter sp.

proof_lines: immobilized enzyme on alkylamine glass beads, pH 7.8, 37°C

proof_lines: immobilized enzyme on arylamine glass beads, pH 7.8, 37°C


enzyme_display_name: 18-hydroxynorfluorocurarine reductase

organism: Strychnos nux-vomica

substrate_name: norfluorocurarine

proof_lines: kcat is 1.754 min(-1) with norfluorocurarine as substrate (PubMed:35794473). kcat is 0.337 min(-1) with 18-OH norfluorocurarine as substrate (PubMed:35794473).

enzyme: 18-hydroxynorfluorocurarine reductase

substrate: norfluorocurarine


substrate_name: 18-OH norfluorocurarine

substrate: 18-OH norfluorocurarine


organism: Escherichia coli (strain K12)

substrate_name: NADH (at pH 7.2 and 15 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor NADH

proof_lines: kcat is 1800 min(-1) for the NADH-dependent reduction of 5,10-methylenetetrahydrofolate (at pH 7.2 and 15 degrees Celsius) (PubMed:9922232). kcat is 1410 min(-1) for the oxidation of NADH by enzyme-bound FAD (at pH 7.2 and 15 degrees Celsiu

substrate: NADH (at pH 7.2 and 15 degrees Celsius)


substrate_name: (6R)-5,10-methylenetetrahydrofolate (at pH 7.2 and 15 degrees Celsius)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F235V/F339L with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines: mutant F235V/F339L, pH not specified in the publication, 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R49K to reconstruct the assayed variant sequence.


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: D-arginine dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: D-arginine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y249F to reconstruct the assayed variant sequence.

enzyme: D-arginine dehydrogenase

substrate: D-arginine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y53F to reconstruct the assayed variant sequence.


organism: Corynebacterium sp. U-96


substrate_name: oxygen

smiles: O=O

substrate: oxygen


organism: Corynebacterium sp.

substrate_name: N-ethylglycine

smiles: CCNCC(=O)O

substrate: N-ethylglycine


substrate_name: N-Methyl-L-alanine

substrate: N-Methyl-L-alanine


substrate_name: sarcosine


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate_name: potassium ferricyanide

substrate: potassium ferricyanide


organism: Escherichia coli

assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADH

proof_lines: mutant E28Q, cosubstrate menadione, pH 7.2, 25°C


substrate_name: menadione

substrate: menadione


proof_lines:
wild-type, pH 7.2, 25°C
wild-type, pH 7.2, 4°C
wild-type, pH 7.2, 15°C


proof_lines: mutant D120N, cosubstrate menadione, pH 7.2, 25°C


proof_lines: mutant D120N, cosubstrate NADH, pH 7.2, 25°C


proof_lines: wild-type, cosubstrate menadione, pH 7.2, 25°C


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.2; cofactor NADPH

proof_lines: Chimera-1, cosubstrate NADPH, pH 7.2, temperature not specified in the publication

proof_lines: Chimera-1, cosubstrate NADH, pH 7.2, temperature not specified in the publication


proof_lines: wild-type, cosubstrate NADH, pH 7.2, temperature not specified in the publication


proof_lines: wild-type, pH 7.2, temperature not specified in the publication


assay_conditions_summary: pH 7.2; 277.15 K; cofactor NADH


proof_lines: wild-type, cosubstrate NADH, pH 7.2, 25°C


organism: Homo sapiens

substrate_name: S-(2-aminoethyl)-L-cysteine ketimine

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

proof_lines:
pH 7.2, 37°C
pH 7.2, temperature 37°C

substrate: S-(2-aminoethyl)-L-cysteine ketimine


proof_lines:
pH 7.2, 37°C
pH 7.2, 37°C, recombinant enzyme


substrate_name: 1-piperideine 2-carboxylate

substrate: 1-piperideine 2-carboxylate


enzyme_display_name: UniProt Q93NH4

organism: Paenarthrobacter nicotinovorans

substrate_name: (S)-nicotine

enzyme: UniProt Q93NH4

substrate: (S)-nicotine


enzyme_display_name: UniProt F8G0P2

organism: Pseudomonas putida

enzyme: UniProt F8G0P2


substrate_name: NADH

assay_conditions_summary: pH 7.2; 288.15 K; cofactor NADH

proof_lines: presence of 0.05 mM genistein, pH 7.2, 37°C


assay_conditions_summary: cofactor NADP+

proof_lines: deuterated, NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme

proof_lines: NAD+-M2+-phopsphate-dependent mitochondrial dehydrogenase-cyclohydrolase enzyme


substrate_name: NADP+

proof_lines: substrate constant: methylenetetrahydrofolate, deuterated, NADP+-dependent bifunctional dehydrogenase-cyclohydrolase domain of the cytoplasmic trifunctional enzyme

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


enzyme_display_name: dihydrobenzophenanthridine oxidase

organism: Eschscholzia californica

substrate_name: Dihydromacarpine

enzyme: dihydrobenzophenanthridine oxidase

substrate: Dihydromacarpine


substrate_name: dihydrochelirubine

substrate: dihydrochelirubine


substrate_name: Dihydrosanguinarine

substrate: Dihydrosanguinarine


enzyme_display_name: L-pipecolate oxidase

organism: Macaca mulatta

substrate_name: L-pipecolic acid

enzyme: L-pipecolate oxidase

substrate: L-pipecolic acid


substrate_name: (S)-1,3-thiazane-4-carboxylic acid

proof_lines: competitive inhibitor that completely inactivates the enzyme

substrate: (S)-1,3-thiazane-4-carboxylic acid


organism: Sanguinaria canadensis


substrate_name: Dihydrochelerythrine

substrate: Dihydrochelerythrine


organism: Papaver somniferum

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: dimethylglycine oxidase

organism: Cylindrocarpon didymum

substrate_name: N,N-dimethylglycine

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

enzyme: dimethylglycine oxidase

substrate: N,N-dimethylglycine


organism: Rhodotorula glutinis


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: (S)-6-hydroxynicotine oxidase

organism: Ochrobactrum sp. SJY1

enzyme: (S)-6-hydroxynicotine oxidase


organism: Macacine alphaherpesvirus 1


organism: Arthrobacter globiformis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y259F to reconstruct the assayed variant sequence.

proof_lines:
mutant Y259F
mutant Y259F, pH 8.5, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H225Q to reconstruct the assayed variant sequence.

proof_lines:
mutant H225Q
mutant H225Q, pH 8.5, 25°C


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

source_databases_merged: brenda oed


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K287M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N166A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y311F to reconstruct the assayed variant sequence.


column_label: Table 1; row Wild-type; substrate section (S)-6-hydroxynornicotine; column kcat (s^-1) raw value 16; column kcat/Kamine (mM^-1 s^-1) raw value 370; column Kamine (mM) raw value 0.064

normalized_value_unit_evidence: kcat normalized_value=16 normalized_unit=s^-1; kcat/Kamine normalized_value=370 normalized_unit=s^-1*mM^-1; Kamine normalized_value=0.064 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=16 raw_unit=s^-1; kcat/Kamine raw_value=370 raw_unit=mM^-1*s^-1; Kamine raw_value=0.064 raw_unit=mM

row_label: Wild-type / (S)-6-hydroxynornicotine

table_label: Table 1. Steady-state kinetic parameters for wild-type and variant L-6-hydroxynicotine oxidase


column_label: Table 1; row Y311F; substrate section (S)-6-hydroxynicotine; column K_O2 (mM); raw value 0.19 mM.

raw_value_unit_evidence: Table 1 row Y311F with (S)-6-hydroxynicotine; K_O2 = 0.19 mM.


column_label: Table 1; row N166A; substrate section (S)-6-hydroxynicotine; column K_O2 (mM); raw value 0.20 mM.

raw_value_unit_evidence: Table 1 row N166A with (S)-6-hydroxynicotine; K_O2 = 0.20 mM.


column_label: Table 1; row Wild-type; substrate section (S)-6-hydroxynicotine; column K_O2 (mM); raw value 0.29 mM.

raw_value_unit_evidence: Table 1 row Wild-type with (S)-6-hydroxynicotine; K_O2 = 0.29 mM.

row_label: Wild-type / O2


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R274A/Y311W/C417W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y311W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


proof_lines:
wild-type, pH 7.4, 22°C
pH 7.0, 25°C, wild-type enzyme


enzyme_display_name: (R)-6-hydroxynicotine oxidase

substrate_name: (R)-nicotine

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

enzyme: (R)-6-hydroxynicotine oxidase

substrate: (R)-nicotine


column_label: Table 1 (Steady-State Kinetic Parameters for Wild-Type and Mutant D-6-Hydroxynicotine oxidase), substrate section '(R)-6-Hydroxynornicotine', enzyme row 'wild-type'; column 'kcat (s^-1)' = 8.1 ± 0.5; column 'kcat/Kamine (mM^-1 s^-1)' = 24 ± 3; column 'Kamine (mM)' = 0.34 ± 0.06. The 'kcat/K(O2) (mM^-1 s^-1)' and 'K(O2) (mM)' columns are empty for this section.

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.1 s^-1; the printed unit is already s^-1, so no unit conversion applies, giving 8.1 s^(-1). Km: printed Table 1 cell 0.34 mM; the printed unit is already mM, so no unit conversion applies, giving 0.34 mM. kcat/Km: 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell 24 mM^-1 s^-1 converts to 24.0 s^-1 mM^-1; the catalog carries the exact quotient of the same two printed cells, 8.1 / 0.34 = 23.823529411764703 s^(-1)*mM^(-1), and 24 is that quotient rounded to the whole-unit precision the paper printed.

raw_value_unit_evidence: Table 1, substrate section '(R)-6-Hydroxynornicotine', enzyme row 'wild-type': column kcat (s^-1) prints 8.1 ± 0.5; column Kamine (mM) prints 0.34 ± 0.06; column kcat/Kamine (mM^-1 s^-1) prints 24 ± 3.

row_label: Table 1, wild-type row in the (R)-6-Hydroxynornicotine section

table_label: Table 1: Steady-State Kinetic Parameters for Wild-Type and Mutant D-6-Hydroxynicotine oxidase (Biochemistry 2019, 58(21):2534-2541)


column_label: Table 1 (Steady-State Kinetic Parameters for Wild-Type and Mutant D-6-Hydroxynicotine oxidase), substrate section '(R)-6-Hydroxynicotine', enzyme row 'wild-type'; column 'kcat (s^-1)' = 77 ± 24 (footnote b); column 'kcat/Kamine (mM^-1 s^-1)' = 380 ± 52 (footnote c); column 'Kamine (mM)' = 0.20 ± 0.03; column 'kcat/K(O2) (mM^-1 s^-1)' = 16 ± 1 (footnote b); column 'K(O2) (mM)' = 4.7 ± 1.7 (footnote b); the second sub-row of the same enzyme row prints the apparent kcat 8.7 ± 0.6 s^-1 and the apparent Kamine 0.023 ± 0.004 mM measured at 250 microM O2 (footnote c).

normalized_value_unit_evidence: kcat: printed Table 1 cell 77 s^-1; the printed unit is already s^-1, so no unit conversion applies, giving 77.0 s^(-1). Km: printed Table 1 cell 0.20 mM; the printed unit is already mM, so no unit conversion applies, giving 0.20 mM. kcat/Km: printed Table 1 cell 380 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so 380 mM^-1 s^-1 converts to 380.0 s^(-1)*mM^(-1), the paper's own fitted catalytic-efficiency value for this row.

raw_value_unit_evidence: Table 1, substrate section '(R)-6-Hydroxynicotine', enzyme row 'wild-type': column kcat (s^-1) prints 77 ± 24; column Kamine (mM) prints 0.20 ± 0.03; column kcat/Kamine (mM^-1 s^-1) prints 380 ± 52.

row_label: Table 1, wild-type row in the (R)-6-Hydroxynicotine section


organism: Shinella sp.

proof_lines: kcat is 7.3 sec(-1) with (S)-6-hydroxynicotine as substrate. kcat is 0.396 sec(-1) with nicotine as substrate (PubMed:25002425). kcat is 5.9 sec(-1) with 6-hydroxynornicotine as substrate (PubMed:27568381).


assay_conditions_summary: pH 9

proof_lines: DMGO1, pH 9.0, temperature not specified in the publication

proof_lines: DMGO2, pH 9.0, temperature not specified in the publication


organism: Schizosaccharomyces pombe

substrate_name: L-proline

substrate: L-proline


substrate_name: L-pipecolate

substrate: L-pipecolate


proof_lines: kcat is 30 sec(-1) with (S)-6-hydroxynicotine as substrate. kcat is 16 sec(-1) with (S)-6-hydroxynornicotine as substrate.


organism: Shinella sp. (strain HZN7)


proof_lines: pH and temperature not specified in the publication


substrate_name: N,N-Dimethylglycine; H2O; O2

substrate: N,N-Dimethylglycine; H2O; O2


substrate_name: O2; L-Pipecolate

substrate: O2; L-Pipecolate


proof_lines: pH 7.0, 25°C, mutant enzyme K287M, cosubstrate: (S)-6-hydroxynicotine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E352Q with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


organism: Oryctolagus cuniculus


substrate_name: (S)-nicotine

substrate: (S)-nicotine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R274A/Y311W/C417W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y311W with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


organism: Zea mays

smiles: CC(=O)NCCCNCCCCNCCCN


smiles: CC(=O)NCCCNCCCCN


enzyme_display_name: Polyamine oxidase 1

substrate_name: dioxygen

enzyme: Polyamine oxidase 1

substrate: dioxygen


substrate_name: spermine

smiles: C(CCNCCCN)CNCCCN

substrate: spermine


substrate_name: spermidine

smiles: C(CCNCCCN)CN

substrate: spermidine


enzyme_display_name: UniProt P50264

organism: Saccharomyces cerevisiae

enzyme: UniProt P50264


organism: Paenarthrobacter nicotinovorans

substrate_name: FAD

assay_conditions_summary: cofactor FAD

proof_lines:
D- and L-6-Hydroxynicotine Oxidase
Arthrobacter oxidans
coenzyme binding

substrate: FAD


proof_lines:
D- and L-6-hydroxynicotine oxidase
Arthrobacter oxidans
6-hydroxynicotine


column_label: Abstract reports rabbit activity was maximal when FAD, phenazine ethosulfate, and glycerol were included in the assay; Kmapp was 0.74+/-0.16 mM.

raw_value_unit_evidence: Km raw_value=0.74+/-0.16 mM raw_unit=mM

row_label: rabbit kidney cortex L-pipecolic acid oxidation

table_label: PubMed XML abstract PMID 2914918


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E350A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E350Q with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.


enzyme_display_name: non-specific polyamine oxidase

organism: Branchiostoma japonicum

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

enzyme: non-specific polyamine oxidase


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


organism: Mus musculus

proof_lines: pH 10.0, 30°C, recombinant wild-type enzyme, with spermine

proof_lines: pH 8.6, 30°C, recombinant wild-type enzyme, with N,N'-dibenzyl-1,4-diaminobutane

proof_lines: pH 10.0, 30°C, recombinant wild-type enzyme and recombinant mutants H64A and H64N, with N1-acetylspermine


proof_lines: pH 8.6, 30°C, recombinant mutants H64A and H64Q, with N,N'-dibenzyl-1,4-diaminobutane


proof_lines: pH 8.6, 30°C, recombinant mutant H64N, with N,N'-dibenzyl-1,4-diaminobutane

proof_lines: pH 10.0, 30°C, recombinant mutant H64N, with N1-acetylspermine

proof_lines: pH 10.0, 30°C, recombinant mutant H64N, with spermine


proof_lines: pH 10.0, 30°C, recombinant mutants H64A and H64Q


proof_lines: pH 10.0, 30°C, recombinant mutants H64A and H64N, with spermine


proof_lines: pH 10.0, 30°C, recombinant mutant H64Q, with spermine

proof_lines: pH 10.0, 30°C, recombinant mutant H64Q, with N1-acetylspermine

proof_lines: pH 8.6, 30°C, recombinant mutant H64Q, with N,N'-dibenzyl-1,4-diaminobutane


proof_lines: pH 10.0, 30°C, recombinant mutant H64A, with N1-acetylspermine

proof_lines: pH 8.6, 30°C, recombinant mutant H64A, with N,N'-dibenzyl-1,4-diaminobutane


proof_lines: pH 8.6, 30°C, recombinant mutants H64A and H64N


proof_lines: pH 8.6, 30°C, recombinant wild-type enzyme


proof_lines: pH 10.0, 30°C, recombinant wild-type enzyme


organism: Oryza sativa

substrate_name: norspermidine

smiles: C(CN)CNCCCN

substrate: norspermidine


substrate_name: thermospermine

smiles: C(CCNCCCNCCCN)CN

substrate: thermospermine


substrate_name: norspermine

smiles: C(CN)CNCCCNCCCN

substrate: norspermine


enzyme_display_name: N1-acetylpolyamine oxidase

enzyme: N1-acetylpolyamine oxidase


enzyme_display_name: spermine oxidase

organism: Ascaris suum

substrate_name: O2; Spermine; H2O

enzyme: spermine oxidase

substrate: O2; Spermine; H2O


substrate_name: tryptamine

substrate: tryptamine


organism: Bos taurus


smiles: C(CN)CNCCNCCCN


proof_lines: pH 7.2, 37°C, with spermine as substrate


substrate_name: O2; H2O; Tryptamine

substrate: O2; H2O; Tryptamine


smiles: CC(=O)NCCCCNCCCN


enzyme_display_name: N-alkylglycine oxidase

organism: Cladosporium sp.

substrate_name: N-ethylglycine

enzyme: N-alkylglycine oxidase

substrate: N-ethylglycine


substrate_name: sarcosine

smiles: CNCC(=O)O

substrate: sarcosine


substrate_name: Nepsilon-carboxymethyllysine

substrate: Nepsilon-carboxymethyllysine


organism: Arabidopsis thaliana


organism: Synechocystis sp. PCC 6803


organism: Acanthamoeba culbertsoni


organism: Mammalia

substrate_name: N1-Acetylspermidine; O2; H2O

substrate: N1-Acetylspermidine; O2; H2O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 9; 303.15 K; buffer of 0

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), spermine block, wild-type PAO column: parameter row 'Ks,app (mM)' = 8; parameter row 'kcat,app (s^-1)' = 8; parameter row 'kcat/Ks (mM^-1 s^-1)' = 1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 8 s^(-1); the exported value is 8.0 s^(-1). Km: printed Table 2 cell 8 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 8 mM; the exported value is 8.0 mM. kcat/Km: printed Table 2 cell 1 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 1 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 8 / 8 = 1.0 s^-1 mM^-1, identical to the printed efficiency cell and to the exported kcat_over_km.

raw_value_unit_evidence: Table 2, spermine block, wild-type PAO column: kcat,app = 8 s^-1; Ks,app = 8 mM; printed kcat/Ks = 1 mM^-1 s^-1.

table_label: Table 2: Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases (Biochemistry 2017, volume 56, number 3, pages 458-467); printed columns wild-type PAO, N313D, N313A, N313L and N313T, each carrying an N1-acetylspermine block and a spermine block of three parameter rows Ks,app (mM), kcat,app (s^-1) and kcat/Ks (mM^-1 s^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N313A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313T to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313T column: parameter row 'Ks,app (mM)' = 0.12; parameter row 'kcat,app (s^-1)' = 22; parameter row 'kcat/Ks (mM^-1 s^-1)' = 175.

normalized_value_unit_evidence: kcat: printed Table 2 cell 22 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 22 s^(-1); the exported value is 22.0 s^(-1). Km: printed Table 2 cell 0.12 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.12 mM; the exported value is 0.12 mM. kcat/Km: printed Table 2 cell 175 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 175 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 22 / 0.12 = 183.33333333333334 s^-1 mM^-1, which is the exported kcat_over_km 183.33333333333334; the printed efficiency cell 175 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313T column: kcat,app = 22 s^-1; Ks,app = 0.12 mM; printed kcat/Ks = 175 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313A column: parameter row 'Ks,app (mM)' = 0.1; parameter row 'kcat,app (s^-1)' = 25; parameter row 'kcat/Ks (mM^-1 s^-1)' = 277.

normalized_value_unit_evidence: kcat: printed Table 2 cell 25 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 25 s^(-1); the exported value is 25.0 s^(-1). Km: printed Table 2 cell 0.1 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.1 mM; the exported value is 0.1 mM. kcat/Km: printed Table 2 cell 277 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 277 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 25 / 0.1 = 250.0 s^-1 mM^-1, which is the exported kcat_over_km 250.0; the printed efficiency cell 277 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313A column: kcat,app = 25 s^-1; Ks,app = 0.1 mM; printed kcat/Ks = 277 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313L to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313L column: parameter row 'Ks,app (mM)' = 0.2; parameter row 'kcat,app (s^-1)' = 25; parameter row 'kcat/Ks (mM^-1 s^-1)' = 144.

normalized_value_unit_evidence: kcat: printed Table 2 cell 25 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 25 s^(-1); the exported value is 25.0 s^(-1). Km: printed Table 2 cell 0.2 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.2 mM; the exported value is 0.2 mM. kcat/Km: printed Table 2 cell 144 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 144 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 25 / 0.2 = 125.0 s^-1 mM^-1, which is the exported kcat_over_km 125.0; the printed efficiency cell 144 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313L column: kcat,app = 25 s^-1; Ks,app = 0.2 mM; printed kcat/Ks = 144 mM^-1 s^-1.


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

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, wild-type PAO column: parameter row 'Ks,app (mM)' = 0.003; parameter row 'kcat,app (s^-1)' = 27; parameter row 'kcat/Ks (mM^-1 s^-1)' = 9600.

normalized_value_unit_evidence: kcat: printed Table 2 cell 27 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 27 s^(-1); the exported value is 27.0 s^(-1). Km: printed Table 2 cell 0.003 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.003 mM; the exported value is 0.003 mM. kcat/Km: printed Table 2 cell 9600 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 9600 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 27 / 0.003 = 9000.0 s^-1 mM^-1, which is the exported kcat_over_km 9000.0; the printed efficiency cell 9600 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, wild-type PAO column: kcat,app = 27 s^-1; Ks,app = 0.003 mM; printed kcat/Ks = 9600 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8C0L6 and applied mutation signature N313D to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for Wild-Type and Mutant Murine Polyamine Oxidases), N1-acetylspermine block, N313D column: parameter row 'Ks,app (mM)' = 0.2; parameter row 'kcat,app (s^-1)' = 27; parameter row 'kcat/Ks (mM^-1 s^-1)' = 137.

normalized_value_unit_evidence: kcat: printed Table 2 cell 27 s^-1 (row kcat,app); the column head prints s^-1, so no unit conversion applies and the paper value is 27 s^(-1); the exported value is 27.0 s^(-1). Km: printed Table 2 cell 0.2 mM (row Ks,app, the apparent Michaelis constant); the column head prints mM, so no unit conversion applies and the paper value is 0.2 mM; the exported value is 0.2 mM. kcat/Km: printed Table 2 cell 137 mM^-1 s^-1 (row kcat/Ks); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the printed cell is 137 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 27 / 0.2 = 135.0 s^-1 mM^-1, which is the exported kcat_over_km 135.0; the printed efficiency cell 137 is the paper's own fitted value and is the value proposed for the catalog.

raw_value_unit_evidence: Table 2, N1-acetylspermine block, N313D column: kcat,app = 27 s^-1; Ks,app = 0.2 mM; printed kcat/Ks = 137 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50264 and applied mutation signature D94N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.35; 298.15 K; buffer containing 10 percent glycerol

column_label: Table 2 (Steady-State Kinetic Parameters), spermine substrate block, value column under the printed head D94N: printed row Kamine (uM) = 320; printed row kcat (s-1) = 2.0; printed row kcat/Kamine (mM-1 s-1) = 4.1. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 104 and KO2 (uM) = 192, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 2.0 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.0 s^(-1). Km: printed Table 2 cell 320 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 320 / 1000 = 0.32 mM. kcat/Km: printed Table 2 cell 4.1 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 4.1 s^(-1)*mM^(-1). The catalog carries kcat 2.0 s^(-1), Km 0.32 mM and kcat_over_km 6.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, spermine block, value column under the printed head D94N: Kamine = 320 uM; kcat = 2.0 s-1; printed kcat/Kamine = 4.1 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, spermine block, D94N column

table_label: Table 2: Steady-State Kinetic Parameters for Wild-type Fmsl and the N195A and D94N Enzymes (Biochemistry 2012, 51(43):8690-8697). Printed parameter rows in each substrate block: kcat (s-1); kcat/Kamine (mM-1 s-1); Kamine (uM); kcat/KO2 (mM-1 s-1); KO2 (uM). Printed value columns, left to right: Fms1 (footnote d, from ref. (13)), N195A, D94N.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50264 and applied mutation signature N195A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-State Kinetic Parameters), spermine substrate block, value column under the printed head N195A: printed row Kamine (uM) = 127; printed row kcat (s-1) = 4.9; printed row kcat/Kamine (mM-1 s-1) = 38.5. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 327 and KO2 (uM) = 15, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 4.9 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 4.9 s^(-1). Km: printed Table 2 cell 127 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 127 / 1000 = 0.127 mM. kcat/Km: printed Table 2 cell 38.5 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 38.5 s^(-1)*mM^(-1). The catalog carries kcat 4.9 s^(-1), Km 0.127 mM and kcat_over_km 38.58267716535433 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, spermine block, value column under the printed head N195A: Kamine = 127 uM; kcat = 4.9 s-1; printed kcat/Kamine = 38.5 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, spermine block, N195A column


assay_conditions_summary: pH 9; 298.15 K; buffer containing 10 percent glycerol

column_label: Table 2 (Steady-State Kinetic Parameters), N1-acetylspermine substrate block, value column under the printed head N195A: printed row Kamine (uM) = 104; printed row kcat (s-1) = 8.1; printed row kcat/Kamine (mM-1 s-1) = 78. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 405 and KO2 (uM) = 20, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8.1 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 8.1 s^(-1). Km: printed Table 2 cell 104 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 104 / 1000 = 0.104 mM. kcat/Km: printed Table 2 cell 78 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 78.0 s^(-1)*mM^(-1). The catalog carries kcat 8.1 s^(-1), Km 0.104 mM and kcat_over_km 77.88461538461539 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, N1-acetylspermine block, value column under the printed head N195A: Kamine = 104 uM; kcat = 8.1 s-1; printed kcat/Kamine = 78 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, N1-acetylspermine block, N195A column


column_label: Table 2 (Steady-State Kinetic Parameters), N1-acetylspermine substrate block, value column under the printed head D94N: printed row Kamine (uM) = 30; printed row kcat (s-1) = 9.7; printed row kcat/Kamine (mM-1 s-1) = 320. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 100 and KO2 (uM) = 97, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.7 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 9.7 s^(-1). Km: printed Table 2 cell 30 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 30 / 1000 = 0.03 mM. kcat/Km: printed Table 2 cell 320 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 320.0 s^(-1)*mM^(-1). The catalog carries kcat 9.7 s^(-1), Km 0.03 mM and kcat_over_km 323.3333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, N1-acetylspermine block, value column under the printed head D94N: Kamine = 30 uM; kcat = 9.7 s-1; printed kcat/Kamine = 320 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, N1-acetylspermine block, D94N column


column_label: Table 2 (Steady-State Kinetic Parameters), N1-acetylspermine substrate block, value column under the printed head Fms1: printed row Kamine (uM) = 10.9; printed row kcat (s-1) = 15.1; printed row kcat/Kamine (mM-1 s-1) = 1400. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 358 and KO2 (uM) = 43.6, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 15.1 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 15.1 s^(-1). Km: printed Table 2 cell 10.9 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 10.9 / 1000 = 0.0109 mM. kcat/Km: printed Table 2 cell 1400 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 1400.0 s^(-1)*mM^(-1). The catalog carries kcat 15.1 s^(-1), Km 0.011 mM and kcat_over_km 1372.7272727272727 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, N1-acetylspermine block, value column under the printed head Fms1: Kamine = 10.9 uM; kcat = 15.1 s-1; printed kcat/Kamine = 1400 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, N1-acetylspermine block, Fms1 wild type column


column_label: Table 2 (Steady-State Kinetic Parameters), spermine substrate block, value column under the printed head Fms1: printed row Kamine (uM) = 118; printed row kcat (s-1) = 39.0; printed row kcat/Kamine (mM-1 s-1) = 330. The value printed after the plus/minus sign in each of those cells is the printed uncertainty and is not an exported metric; the same column also prints kcat/KO2 (mM-1 s-1) = 428 and KO2 (uM) = 91, which are the oxygen parameters of the same table line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 39.0 in a row headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 39.0 s^(-1). Km: printed Table 2 cell 118 in a row headed Kamine (uM); 1 uM is 0.001 mM, so 118 / 1000 = 0.118 mM. kcat/Km: printed Table 2 cell 330 in a row headed kcat/Kamine (mM-1 s-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no unit conversion applies and the value is 330.0 s^(-1)*mM^(-1). The catalog carries kcat 39.0 s^(-1), Km 0.118 mM and kcat_over_km 330.5084745762712 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, spermine block, value column under the printed head Fms1: Kamine = 118 uM; kcat = 39.0 s-1; printed kcat/Kamine = 330 in a row headed kcat/Kamine (mM-1 s-1).

row_label: Table 2, spermine block, Fms1 wild type column


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N195A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 25°C, recombinant mutant N195A, with spermine

proof_lines: pH 9.0, 25°C, recombinant mutant N195A, with N1-acetylspermine


proof_lines: pH 9.0, 25°C, recombinant wild-type Fms1, with N1-acetylspermine

proof_lines: pH 9.0, 25°C, recombinant wild-type Fms1, with spermine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D94N to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 25°C, recombinant mutant D94N, with N1-acetylspermine

proof_lines: pH 9.0, 25°C, recombinant mutant D94N, with spermine


organism: Homo sapiens


substrate_name: alpha-methylspermidine

smiles: CC(CCNCCCCN)N

substrate: alpha-methylspermidine


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

assay_conditions_summary: pH 6


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O64411 and applied mutation signature E62Q with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 298.15 K; buffer Pichia pastoris | 0.2 M sodium phosphate

column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Glu62Gln; columns kcat (spm) (s^-1) and Km (spm) (uM); kcat (spm) cell = 2.8; Km (spm) cell = 14.7; Table 1 has no kcat/Km (spm) column. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermine (spm) | Glu62Gln MPAO, the site-directed Glu62Gln mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Glu62Gln, kcat (spm) = 2.8 s^-1 | Table 1, row Glu62Gln, Km (spm) = 14.7 uM | kcat/Km (spm): Table 1 prints no kcat/Km (spm) column and this article prints no kcat/Km value for spm oxidation by this enzyme form

normalized_value_unit_evidence: Km: printed Table 1 Km (spm) cell 14.7 uM; 1 uM is 1/1000 mM, so 14.7 / 1000 = 0.0147 mM; the export stores 0.0147 mM. kcat: printed Table 1 kcat (spm) cell 2.8 s^-1; already in s^-1, no unit conversion applies; the export stores 2.8 s^(-1). kcat/Km: Table 1 prints no kcat/Km (spm) cell; the quotient of the two printed cells is 2.8 / 0.0147 = 190.47619047619048 s^-1 mM^-1, which is the exported 190.47619047619048 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Glu62Gln: kcat (spm) = 2.8 s^-1; Km (spm) = 14.7 uM; Table 1 prints no kcat/Km (spm) column.

row_label: Table 1, MPAO row Glu62Gln


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O64411 and applied mutation signature E170Q with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Glu170Gln; columns kcat (spm) (s^-1) and Km (spm) (uM); kcat (spm) cell = 4.6; Km (spm) cell = 12.5; Table 1 has no kcat/Km (spm) column. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermine (spm) | Glu170Gln MPAO, the site-directed Glu170Gln mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Glu170Gln, kcat (spm) = 4.6 s^-1 | Table 1, row Glu170Gln, Km (spm) = 12.5 uM | kcat/Km (spm): Table 1 prints no kcat/Km (spm) column and this article prints no kcat/Km value for spm oxidation by this enzyme form

normalized_value_unit_evidence: Km: printed Table 1 Km (spm) cell 12.5 uM; 1 uM is 1/1000 mM, so 12.5 / 1000 = 0.0125 mM; the export stores 0.0125 mM. kcat: printed Table 1 kcat (spm) cell 4.6 s^-1; already in s^-1, no unit conversion applies; the export stores 4.6 s^(-1). kcat/Km: Table 1 prints no kcat/Km (spm) cell; the quotient of the two printed cells is 4.6 / 0.0125 = 367.99999999999994 s^-1 mM^-1, which is the exported 367.99999999999994 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Glu170Gln: kcat (spm) = 4.6 s^-1; Km (spm) = 12.5 uM; Table 1 prints no kcat/Km (spm) column.

row_label: Table 1, MPAO row Glu170Gln


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O64411 and applied mutation signature Y298F with inferred residue-numbering offset +28 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Tyr298Phe; columns kcat (spm) (s^-1) and Km (spm) (uM); kcat (spm) cell = 7.7; Km (spm) cell = 1.2; Table 1 has no kcat/Km (spm) column. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermine (spm) | Tyr298Phe MPAO, the site-directed Tyr298Phe mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Tyr298Phe, kcat (spm) = 7.7 s^-1 | Table 1, row Tyr298Phe, Km (spm) = 1.2 uM | kcat/Km (spm): Table 1 prints no kcat/Km (spm) column and this article prints no kcat/Km value for spm oxidation by this enzyme form

normalized_value_unit_evidence: Km: printed Table 1 Km (spm) cell 1.2 uM; 1 uM is 1/1000 mM, so 1.2 / 1000 = 0.0012 mM; the export stores 0.0012 mM. kcat: printed Table 1 kcat (spm) cell 7.7 s^-1; already in s^-1, no unit conversion applies; the export stores 7.7 s^(-1). kcat/Km: Table 1 prints no kcat/Km (spm) cell; the quotient of the two printed cells is 7.7 / 0.0012 = 6416.666666666667 s^-1 mM^-1, which is the exported 6416.666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Tyr298Phe: kcat (spm) = 7.7 s^-1; Km (spm) = 1.2 uM; Table 1 prints no kcat/Km (spm) column.

row_label: Table 1, MPAO row Tyr298Phe


column_label: Table 1: Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris (Biochemistry 2005, 44(49): 16108-16120; journal page 16112, PDF page 5); printed column heads MPAO | kcat (spd) (s^-1) | kcat (spm) (s^-1) | kcat (spd)/kcat (spm) | Km (spd) (uM) | Km (spm) (uM) | kcat/Km (spd) (s^-1 uM^-1). Table 1, MPAO row Glu62Gln; columns kcat (spd) (s^-1), Km (spd) (uM) and kcat/Km (spd) (s^-1 uM^-1); kcat (spd) cell = 8.3; Km (spd) cell = 24.6; kcat/Km (spd) cell = 0.3. captured primary segment: Table 1 (Kinetic Constants of spd and spm Oxidation by Wild-Type and Mutant Forms of MPAO Expressed in P. pastoris), journal page 16112 (PDF page 5) | spermidine (spd) | Glu62Gln MPAO, the site-directed Glu62Gln mutant of recombinant Zea mays polyamine oxidase expressed in Pichia pastoris | 0.2 M sodium phosphate buffer at pH 6.0, 25 °C, O2 at the air-saturated level | Table 1, row Glu62Gln, kcat (spd) = 8.3 s^-1 | Table 1, row Glu62Gln, Km (spd) = 24.6 uM | Table 1, row Glu62Gln, kcat/Km (spd) = 0.3 s^-1 uM^-1

normalized_value_unit_evidence: Km: printed Table 1 Km (spd) cell 24.6 uM; 1 uM is 1/1000 mM, so 24.6 / 1000 = 0.0246 mM; the export stores 0.0246 mM. kcat: printed Table 1 kcat (spd) cell 8.3 s^-1; already in s^-1, no unit conversion applies; the export stores 8.3 s^(-1). kcat/Km: printed Table 1 kcat/Km (spd) cell 0.3 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.3 x 1000 = 300.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 8.3 / 0.0246 = 337.3983739837399 s^-1 mM^-1, against the printed catalytic-efficiency cell 300.0 s^-1 mM^-1, which is that quotient rounded to the one decimal the column prints; the export stores 337.3983739837399 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 16112, Table 1, MPAO row Glu62Gln: kcat (spd) = 8.3 s^-1; Km (spd) = 24.6 uM; printed kcat/Km (spd) = 0.3 s^-1 uM^-1.