substrate_name: alpha-D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)


organism: Bacillus subtilis (strain 168)

substrate_name: D-xylose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 9

data_origin: experimental

status: unverified

source: uniprot


enzyme_display_name: scyllo-inositol 2-dehydrogenase (NAD+)

organism: Bacillus subtilis

substrate_name: NADH

source_db: brenda

verification_status: verified

sequence_source: multiple

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

column_label: Table 4 reports IolX-(His)6, varied substrate NADH, constant substrate 10 mM SIS, K m = 0.019 +/- 0.007 mM; normalized Km = 0.019 mM.

normalized_value_unit_evidence: Km=0.019 mM; Table 4 reports values directly in mM.

row_label: IolX-(His)6 / varied substrate NADH / K m column

table_label: Table 4 / Km and Vmax values for purified IolX-(His)6 and IolW-(His)6

source_databases_merged: brenda uniprot

enzyme: scyllo-inositol 2-dehydrogenase (NAD+)

substrate: NADH

status: verified

source: brenda


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

column_label: Table 4 reports IolX-(His)6, varied substrate NAD+, constant substrate 60 mM SI, K m = 0.15 +/- 0.01 mM; normalized Km = 0.15 mM.

normalized_value_unit_evidence: Km=0.15 mM; Table 4 reports values directly in mM.

row_label: IolX-(His)6 / varied substrate NAD+ / K m column

substrate: NAD+


substrate_name: scyllo-inosose

column_label: Table 4 reports IolX-(His)6, varied substrate SIS, constant substrate 0.5 mM NADH, K m = 2.85 +/- 0.48 mM; normalized Km = 2.85 mM.

normalized_value_unit_evidence: Km=2.85 mM; Table 4 reports values directly in mM.

row_label: IolX-(His)6 / varied substrate SIS / K m column

substrate: scyllo-inosose


substrate_name: scyllo-Inositol

column_label: Table 4 reports IolX-(His)6, varied substrate SI, constant substrate 0.5 mM NAD+, K m = 17.1 +/- 0.24 mM; normalized Km = 17.1 mM.

normalized_value_unit_evidence: Km=17.1 mM; Table 4 reports values directly in mM.

row_label: IolX-(His)6 / varied substrate SI / K m column

substrate: scyllo-Inositol


enzyme_display_name: farnesol dehydrogenase (NAD+)

organism: Carpoglyphus lactis

substrate_name: geraniol

kcat_over_km_origin: calculated

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

enzyme: farnesol dehydrogenase (NAD+)

substrate: geraniol


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+

column_label: Abstract reports Km values for geraniol and NAD+ were 51.0 microM and 59.5 microM respectively.

raw_value_unit_evidence: Km raw_value=59.5 microM raw_unit=microM

row_label: Carpoglyphus lactis geraniol dehydrogenase / NAD+

table_label: PubMed XML abstract PMID 18422649


enzyme_display_name: farnesol dehydrogenase (NAD(+))

source_db: oed

sequence: MVQNPGASAIQCRAAVLRKEGQPMKIEQVLIQA

wild_type_sequence: MVQNPGASAIQCRAAVLRKEGQPMKIEQVLIQA

smiles: CC(C)=CCC/C(C)=C/CO

enzyme: farnesol dehydrogenase (NAD(+))

source: oed


enzyme_display_name: scyllo-inositol 2-dehydrogenase (NADP(+)) IolW

substrate_name: NADP(+)

assay_conditions_summary: cofactor NADP+

column_label: Table 4 reports IolW-(His)6, varied substrate NADP+, constant substrate 60 mM SI, K m = 0.096 +/- 0.015 mM; normalized Km = 0.096 mM.

normalized_value_unit_evidence: Km=0.096 mM; Table 4 reports values directly in mM.

row_label: IolW-(His)6 / varied substrate NADP+ / K m column

substrate: NADP(+)


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

column_label: Table 4 reports IolW-(His)6, varied substrate NADPH, constant substrate 10 mM SIS, K m = 0.027 +/- 0.008 mM; normalized Km = 0.027 mM.

normalized_value_unit_evidence: Km=0.027 mM; Table 4 reports values directly in mM.

row_label: IolW-(His)6 / varied substrate NADPH / K m column

enzyme: scyllo-inositol 2-dehydrogenase (NADP(+)) IolW

substrate: NADPH


enzyme_display_name: UniProt P77398

organism: Escherichia coli

source_db: skid

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=8

source_databases_merged: skid uniprot

enzyme: UniProt P77398

source: skid


enzyme_display_name: (R)-mandelate dehydrogenase

organism: Schleiferilactobacillus harbinensis

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

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+

enzyme: (R)-mandelate dehydrogenase


substrate_name: (R)-mandelate

substrate: (R)-mandelate


enzyme_display_name: ketol-acid reductoisomerase [NAD(P)+]

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

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: mutant A71S/R76D/S78D/Q110A, pH 7.0, temperature not specified in the publication

enzyme: ketol-acid reductoisomerase [NAD(P)+]


assay_conditions_summary: pH 7; cofactor NADH

proof_lines: mutant S78D/Q110V, pH 7.0, temperature not specified in the publication


mutation_type: substitution

proof_lines: mutant S78D, pH 7.0, temperature not specified in the publication


proof_lines: mutant Q110A, pH 7.0, temperature not specified in the publication


proof_lines: mutant Q110V, pH 7.0, temperature not specified in the publication


proof_lines: mutant A71S/R76D/S78D/Q110V, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant A71S/R76D/S78D/Q110V, pH 7.0, temperature not specified in the publication


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

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


proof_lines: mutant A71S/R76D/S78D/Q110V/D146G/G185R/K433E , pH not specified in the publication, temperature not specified in the publication


assay_conditions_summary: cofactor NADH


organism: Shewanella sp.

proof_lines: mutant R76D/Ser78D, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant A71S/R76D/S78AD/Q110V, pH not specified in the publication, temperature not specified in the publication


organism: Rhodotorula graminis

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: pH 5.9, temperature not specified in the publication

substrate: Unknown


assay_conditions_summary: pH 9.5; 300.15 K; cofactor NADH


substrate_name: phenylglyoxylate

substrate: phenylglyoxylate


assay_conditions_summary: pH 9.5; 300.15 K; cofactor NAD+


enzyme_display_name: L-rhamnose 1-dehydrogenase [NAD(P)+]

organism: Azotobacter vinelandii

substrate_name: L-Mannose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F99Y to reconstruct the assayed variant sequence.

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

enzyme: L-rhamnose 1-dehydrogenase [NAD(P)+]

substrate: L-Mannose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature F99A to reconstruct the assayed variant sequence.


substrate_name: L-rhamnose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q156A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

substrate: L-rhamnose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature I196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature T191F with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


substrate_name: L-Lyxose

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

substrate: L-Lyxose


proof_lines: recombinant wild-type enzyme, pH 9.0, 30°C


substrate_name: NADP+

assay_conditions_summary: pH 9; cofactor NADP+

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D200H to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 9; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S37H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D200A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R15T to reconstruct the assayed variant sequence.


enzyme_display_name: L-arabinose 1-dehydrogenase [NAD(P)+]

organism: Azospirillum brasilense

substrate_name: L-arabinose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173S to reconstruct the assayed variant sequence.

proof_lines:
pH 9.0, 30°C, mutant enzyme N173S
30°C, pH 9.0, mutant enzyme N173S

enzyme: L-arabinose 1-dehydrogenase [NAD(P)+]

substrate: L-arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173A to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme N173A
pH 9.0, 30°C, mutant enzyme N173A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173Q to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme N173Q
pH 9.0, 30°C, mutant enzyme N173Q


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S37D/R38A to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme S37D/R38A
pH 9.0, 30°C, mutant enzyme S37D/R38A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173G to reconstruct the assayed variant sequence.

proof_lines:
pH 9.0, 30°C, mutant enzyme N173G
30°C, pH 9.0, mutant enzyme N173G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N173V to reconstruct the assayed variant sequence.

proof_lines:
pH 9.0, 30°C, mutant enzyme N173V
30°C, pH 9.0, mutant enzyme N173V


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W152Y to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W152Y
pH 9.0, 30°C, mutant enzyme W152Y


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H119N to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme H119N
pH 9.0, 30°C, mutant enzyme H119N


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

proof_lines:
30°C, pH 9.0, wild-type enzyme
pH 9.0, 30°C, wild-type enzyme enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W152F to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W152F
pH 9.0, 30°C, mutant enzyme W152F


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S37D to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme S37D
pH 9.0, 30°C, mutant enzyme S37D


proof_lines:
30°C, pH 9.0, wild-type enzyme
pH 9.0, 30°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W152H to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W152H
pH 9.0, 30°C, mutant enzyme W152H


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R38A to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme R38A
pH 9.0, 30°C, mutant enzyme R38A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W152A to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W152A
pH 9.0, 30°C, mutant enzyme W152A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W231A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines:
30°C, pH 9.0, mutant enzyme W231A
pH 9.0, 30°C, mutant enzyme W231A


enzyme_display_name: ketol-acid reductoisomerase (NAD+)

organism: Archaeoglobus fulgidus

proof_lines: pH 7, temperature not specified in the publication, cosubstrate: (2S)-2-hydroxy-2-methyl-3-oxobutanoate

enzyme: ketol-acid reductoisomerase (NAD+)


enzyme_display_name: L-rhamnose 1-dehydrogenase (NADP+)

organism: Thermoplasma acidophilum

assay_conditions_summary: pH 7

proof_lines: kcat is 1.341 min(-1) for dehydrogenase activity with L-rhamnose as substrate (at pH 7 and 60 degrees Celsius). kcat is 1.426 min(-1) for dehydrogenase activity with L-lyxose as substrate (at pH 7 and 60 degrees Celsius). kcat is 892.9 min(

enzyme: L-rhamnose 1-dehydrogenase (NADP+)


assay_conditions_summary: pH 7; cofactor NADP+

proof_lines:
pH 7.0, 60°C, cosubstrate: L-lyxose
pH 7.0, 60°C, cosubstrate: L-rhamnose
pH 7.0, 60°C, cosubstrate: L-mannose


enzyme_display_name: NADP-dependent 3-hydroxy acid dehydrogenase YdfG

organism: Escherichia coli (strain K12)

substrate_name: NADP(+) (at pH 9 and at 30 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: The highest catalytic efficiency was observed with L-allo-threonine.


substrate_name: L-serine (at pH 9 and at 30 degrees Celsius)

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

enzyme: NADP-dependent 3-hydroxy acid dehydrogenase YdfG


substrate_name: D-threonine (at pH 9 and at 30 degrees Celsius)

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


substrate_name: L-glycerate (at pH 9 and at 30 degrees Celsius)

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


substrate_name: D-glycerate (at pH 9 and at 30 degrees Celsius)


enzyme_display_name: Ketol-acid reductoisomerase (NAD(+))

organism: Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 26808 / PB)

substrate_name: NADH (at pH 7 with S2AL as substrate)

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.

proof_lines: kcat is 0.46 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate). kcat is 0.25 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate).

enzyme: Ketol-acid reductoisomerase (NAD(+))

substrate: NADH (at pH 7 with S2AL as substrate)


substrate_name: NADPH (at pH 7 with S2AL as substrate)

substrate: NADPH (at pH 7 with S2AL as substrate)


organism: Haloferax volcanii

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

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: pH 8.0, temperature not specified in the publication


substrate_name: D-galactose

assay_conditions_summary: pH 8

substrate: D-galactose


organism: Slackia exigua

substrate_name: NADPH

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_accession:D0WGK0 and applied mutation signature S61D/S63D to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Se_KARI DD / NADPH; columns KM for cofactors [uM] / NADPH, kcat for cofactors [s^-1] / NADPH, and kcat/KM [mM^-1 s^-1] / NADPH; Se_KARI DD / NADPH: KM 880 uM; kcat 0.10 s^-1; kcat/KM 0.11 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.88 mM; kcat=0.10 s^-1; kcat/Km=0.11 s^-1*mM^-1.

row_label: Se_KARI DD / NADPH

status: corrected


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

proof_lines: mutant S61D/S63D/I95V, pH not specified in the publication, temperature not specified in the publication


substrate_name: NADH

column_label: Table 1 row Se_KARI / mutations column dash; K_M for cofactors [uM] / NADH = 45; kcat for cofactors [s^-1] / NADH = 0.41; kcat/K_M [mM^-1 s^-1] / NADH = 9.

normalized_value_unit_evidence: Km normalized_value=0.045 normalized_unit=mM; kcat normalized_value=0.41 normalized_unit=s^-1; kcat/Km normalized_value=9 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=45 raw_unit=uM for NADH; kcat raw_value=0.41 raw_unit=s^-1 for NADH; kcat/Km raw_value=9 raw_unit=mM^-1 s^-1 for NADH.

row_label: Se_KARI / mutations column dash

table_label: PMC3704004 Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and variants

substrate: NADH


column_label: Table 1 row Se_KARI / mutations column dash; K_M for cofactors [uM] / NADPH = 1; kcat for cofactors [s^-1] / NADPH = 0.8; kcat/K_M [mM^-1 s^-1] / NADPH = 800.

normalized_value_unit_evidence: Km normalized_value=0.001 normalized_unit=mM; kcat normalized_value=0.8 normalized_unit=s^-1; kcat/Km normalized_value=800 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=1 raw_unit=uM for NADPH; kcat raw_value=0.8 raw_unit=s^-1 for NADPH; kcat/Km raw_value=800 raw_unit=mM^-1 s^-1 for NADPH.


column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Se_KARI DD / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Se_KARI DD / NADH: KM 113 uM; kcat 0.97 s^-1; kcat/KM 9 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.113 mM; kcat=0.97 s^-1; kcat/Km=9 s^-1*mM^-1.

row_label: Se_KARI DD / NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession:D0WGK0 and applied mutation signature S61D/S63D/I95V to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Se_KARI DDV / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Se_KARI DDV / NADH: KM 47 uM; kcat 1.01 s^-1; kcat/KM 22 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.047 mM; kcat=1.01 s^-1; kcat/Km=22 s^-1*mM^-1.

row_label: Se_KARI DDV / NADH


organism: Hydrogenobaculum sp. Y04AAS1


enzyme_display_name: L-rhamnose 1-dehydrogenase (NAD(P)(+))

organism: Azotobacter vinelandii (strain DJ / ATCC BAA-1303)

substrate_name: NAD(+)

proof_lines: kcat is 2230 min(-1) with L-rhamnose as substrate (in the presence of NAD(+)) (PubMed:18505728). kcat is 4490 min(-1) with L-rhamnose as substrate (in the presence of NADP(+)) (PubMed:18505728). kcat is 5010 min(-1) with L-rhamnose as subst

enzyme: L-rhamnose 1-dehydrogenase (NAD(P)(+))

substrate: NAD(+)


substrate_name: NADP(+)


enzyme_display_name: Ketol-acid reductoisomerase (NAD(P)(+))

organism: Hydrogenobaculum sp. (strain Y04AAS1)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

proof_lines: kcat is 0.12 sec(-1) for isomerase activity with NADPH (at pH 7 with S2AL as substrate). kcat is 0.12 sec(-1) for isomerase activity with NADH (at pH 7 with S2AL as substrate).

enzyme: Ketol-acid reductoisomerase (NAD(P)(+))


organism: Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)

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

proof_lines: kcat is 0.28 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate). kcat is 0.22 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N172A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A

proof_lines: pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A


substrate_name: D-talose

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines: pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense

proof_lines: pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense

source_databases_merged: brenda skid

substrate: D-talose


substrate_name: D-xylose

substrate: D-xylose


proof_lines: pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme

proof_lines: pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme


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

proof_lines: mutant S61D/S63D, pH not specified in the publication, temperature not specified in the publication


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

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


organism: Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A to reconstruct the assayed variant sequence.

proof_lines: kcat is 0.07 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate). kcat is 0.06 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate).


organism: uncultured archaeon

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

proof_lines: pH 7, temperature not specified in the publication, cosubstrate: (2S)-2-hydroxy-2-methyl-3-oxobutanoate


substrate_name: L-fucose

substrate: L-fucose


substrate_name: L-Mannose


substrate_name: L-Lyxose


enzyme_display_name: 3-hydroxy acid dehydrogenase

organism: Saccharomyces cerevisiae

substrate_name: D-serine

proof_lines: The highest catalytic efficiency was observed with L-allo-threonine.

enzyme: 3-hydroxy acid dehydrogenase

substrate: D-serine


substrate_name: L-allo-threonine

substrate: L-allo-threonine


organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

proof_lines: kcat is 0.1 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate). kcat is 0.04 sec(-1) for reductoisomerase activity with NADPH (at pH 7 with S2AL as substrate).


enzyme_display_name: NADP-dependent 3-hydroxy acid dehydrogenase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NADP(+) (at pH 9 and at 30 degrees Celsius)


organism: Desulfosudis oleivorans


organism: Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: kcat is 0.25 sec(-1) for reductoisomerase activity with NADH (at pH 7 with S2AL as substrate).


enzyme_display_name: L-arabinose 1-dehydrogenase [NAD(P)(+)]

organism: Azospirillum brasilense

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R38A to reconstruct the assayed variant sequence.

enzyme: L-arabinose 1-dehydrogenase [NAD(P)(+)]

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S37D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S37D/R38A to reconstruct the assayed variant sequence.


substrate_name: NADP+


substrate_name: L-Arabinose

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H119N to reconstruct the assayed variant sequence.

substrate: L-Arabinose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173Q to reconstruct the assayed variant sequence.


organism: Thermacetogenium phaeum


organism: Lactococcus lactis subsp. lactis

sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q02138 and applied mutation signature V48L/R49P/K52E/S53D to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI LPED / NADPH; columns KM for cofactors [uM] / NADPH, kcat for cofactors [s^-1] / NADPH, and kcat/KM [mM^-1 s^-1] / NADPH; Ll_KARI LPED / NADPH: KM 1,180 uM; kcat 0.06 s^-1; kcat/KM 0.05 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=1.18 mM; kcat=0.06 s^-1; kcat/Km=0.05 s^-1*mM^-1.

row_label: Ll_KARI LPED / NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q02138 and applied mutation signature V48L/R49P/K52L/S53D to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI LPLD / NADPH; columns KM for cofactors [uM] / NADPH, kcat for cofactors [s^-1] / NADPH, and kcat/KM [mM^-1 s^-1] / NADPH; Ll_KARI LPLD / NADPH: KM 1,000 uM; kcat 0.08 s^-1; kcat/KM 0.08 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=1.0 mM; kcat=0.08 s^-1; kcat/Km=0.08 s^-1*mM^-1.

row_label: Ll_KARI LPLD / NADPH


column_label: Table 1 row Ll_KARI / mutations column dash; K_M for cofactors [uM] / NADH = 285; kcat for cofactors [s^-1] / NADH = 0.1; kcat/K_M [mM^-1 s^-1] / NADH = 0.43.

normalized_value_unit_evidence: Km normalized_value=0.285 normalized_unit=mM; kcat normalized_value=0.1 normalized_unit=s^-1; kcat/Km normalized_value=0.43 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=285 raw_unit=uM for NADH; kcat raw_value=0.1 raw_unit=s^-1 for NADH; kcat/Km raw_value=0.43 raw_unit=mM^-1 s^-1 for NADH.

row_label: Ll_KARI / mutations column dash


column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI LPED / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Ll_KARI LPED / NADH: KM 128 uM; kcat 0.35 s^-1; kcat/KM 2.7 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.128 mM; kcat=0.35 s^-1; kcat/Km=2.7 s^-1*mM^-1.

row_label: Ll_KARI LPED / NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q02138 and applied mutation signature V48L/R49P/K52L/S53D/E59K/T182S/E320K to reconstruct the assayed variant sequence.

column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI 2G6 / NADPH; columns KM for cofactors [uM] / NADPH, kcat for cofactors [s^-1] / NADPH, and kcat/KM [mM^-1 s^-1] / NADPH; Ll_KARI 2G6 / NADPH: KM 749 uM; kcat 0.35 s^-1; kcat/KM 0.47 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.749 mM; kcat=0.35 s^-1; kcat/Km=0.47 s^-1*mM^-1.

row_label: Ll_KARI 2G6 / NADPH


column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI LPLD / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Ll_KARI LPLD / NADH: KM 108 uM; kcat 0.40 s^-1; kcat/KM 3.7 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.108 mM; kcat=0.40 s^-1; kcat/Km=3.7 s^-1*mM^-1.

row_label: Ll_KARI LPLD / NADH


column_label: Table 1 row Ll_KARI / mutations column dash; K_M for cofactors [uM] / NADPH = 13; kcat for cofactors [s^-1] / NADPH = 0.8; kcat/K_M [mM^-1 s^-1] / NADPH = 65.

normalized_value_unit_evidence: Km normalized_value=0.013 normalized_unit=mM; kcat normalized_value=0.8 normalized_unit=s^-1; kcat/Km normalized_value=65 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Km raw_value=13 raw_unit=uM for NADPH; kcat raw_value=0.8 raw_unit=s^-1 for NADPH; kcat/Km raw_value=65 raw_unit=mM^-1 s^-1 for NADPH.


column_label: Table 1. Biochemical properties of Ec_IlvC, Sh_KARI, Se_KARI, Ma_KARI, Ll_KARI, Aa_KARI, and their cofactor-switched variants; row Ll_KARI 2G6 / NADH; columns KM for cofactors [uM] / NADH, kcat for cofactors [s^-1] / NADH, and kcat/KM [mM^-1 s^-1] / NADH; Ll_KARI 2G6 / NADH: KM 15 uM; kcat 1.07 s^-1; kcat/KM 71 mM^-1*s^-1. Only Km is unit-converted by dividing by 1000: Km=0.015 mM; kcat=1.07 s^-1; kcat/Km=71 s^-1*mM^-1.

row_label: Ll_KARI 2G6 / NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N173V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W152Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W231A to reconstruct the assayed variant sequence.


organism: Escherichia coli

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

proof_lines: D-serine YdfG


substrate_name: D-Threonine

substrate: D-Threonine


substrate_name: L-Glycerate

substrate: L-Glycerate


substrate_name: L-serine

substrate: L-serine


substrate_name: L-allo-Threonine

substrate: L-allo-Threonine


substrate_name: D-Glycerate

substrate: D-Glycerate


organism: Bacillus subtilis (strain 168)

substrate_name: scyllo-inositol

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

column_label: Table 4 reports IolW-(His)6, varied substrate SI, constant substrate 0.5 mM NADP+, K m = 34.3 +/- 4.4 mM; normalized Km = 34.3 mM.

normalized_value_unit_evidence: Km=34.3 mM; Table 4 reports values directly in mM.

row_label: IolW-(His)6 / varied substrate SI / K m column

substrate: scyllo-inositol


substrate_name: scyllo-inosose

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

column_label: Table 4 reports IolW-(His)6, varied substrate SIS, constant substrate 0.5 mM NADPH, K m = 1.68 +/- 0.16 mM; normalized Km = 1.68 mM.

normalized_value_unit_evidence: Km=1.68 mM; Table 4 reports values directly in mM.

row_label: IolW-(His)6 / varied substrate SIS / K m column

substrate: scyllo-inosose


substrate_name: NADP(+)

column_label: Table 4 reports IolW-(His)6, varied substrate NADP+, constant substrate 60 mM SI, K m = 0.096 +/- 0.015 mM; normalized Km = 0.096 mM.

substrate: NADP(+)


substrate_name: NADPH

column_label: Table 4 reports IolW-(His)6, varied substrate NADPH, constant substrate 10 mM SIS, K m = 0.027 +/- 0.008 mM; normalized Km = 0.027 mM.


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=8


substrate_name: D-Galactose

substrate: D-Galactose


enzyme_display_name: L-arabinose 1-dehydrogenase (NAD(P)(+))

substrate_name: NADP(+) (at 30 degrees Celsius and pH 9.0)

assay_conditions_summary: cofactor NADP+

enzyme: L-arabinose 1-dehydrogenase (NAD(P)(+))


organism: Mycolicibacterium smegmatis

substrate_name: mycothiol

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

column_label: Table 2, formaldehyde dehydrogenase (a), reports K MSH (uM) = 17.3 +/- 0.8.

raw_value_unit_evidence: Km raw_value=17.3 raw_unit=uM

row_label: Formaldehyde dehydrogenase (a)

table_label: Table 2 - Kinetic parameters for the formaldehyde dehydrogenase (a) and MSNO (b) reductase reactions

substrate: mycothiol


assay_conditions_summary: pH 8.7; cofactor NAD+

column_label: Table 2, formaldehyde dehydrogenase (a), reports K NAD (uM) = 354 +/- 16.

raw_value_unit_evidence: Km raw_value=354 raw_unit=uM


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Sungouiella intermedia

substrate_name: oenanthaldehyde

smiles: CCCCCCC=O

assay_conditions_summary: pH 7; cofactor NADH

column_label: Official PMC PDF page 5 (journal page 105), Table 4, Oenanthaldehyde row under Candida intermedia II, columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat=4.6 s^-1; Km=4.7 mM; printed kcat/Km=0.979 s^-1 mM^-1. The exported 0.978723404255319 is the same-row 4.6/4.7 quotient before table rounding.

raw_value_unit_evidence: Table 4, Candida intermedia II, Oenanthaldehyde: kcat=4.6 +/- 0.2 s^-1; Km=4.7 +/- 1.1 mM; kcat/Km=979 M^-1 s^-1.

row_label: Oenanthaldehyde; Candida intermedia II

table_label: Table 4. Kinetic parameters for NADH-dependent reduction of glucose derivatives and other aldehydes by yALR

enzyme: D-xylose reductase [NAD(P)H]

substrate: oenanthaldehyde


substrate_name: D-galactose

column_label: Official PMC PDF page 5 (journal page 105), Table 4, Galactose row under Candida intermedia II, columns kcat, Km, and kcat/Km.

normalized_value_unit_evidence: kcat=5.9 s^-1; Km=74 mM; printed kcat/Km=0.080 s^-1 mM^-1. The exported 0.07972972972972973 is the same-row 5.9/74 quotient before table rounding.

raw_value_unit_evidence: Table 4, Candida intermedia II, Galactose: kcat=5.9 +/- 0.1 s^-1; Km=74 +/- 4 mM; kcat/Km=80 M^-1 s^-1.

row_label: Galactose; Candida intermedia II

substrate: D-galactose


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: NAD(+)-dependent decarboxylation of UDP-glucuronic acid to UDP-4-keto-arabinose


substrate_name: UDP-glucuronate

substrate: UDP-glucuronate


substrate_name: NADP+

substrate: NADP+


proof_lines:
preferred NADP+ to NAD+ as a coenzyme
purified enzyme
Azospirillum brasilense

source_databases_merged: brenda skid uniprot

substrate: NAD+


substrate_name: D-serine

column_label: Official ScienceDirect HTML Table 4 row d-Serine gives YMR226C (B) kcat 7.84 s^-1, Km 71 mM, and Vmax/Km 110 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=7.84 normalized_unit=s^-1; Km normalized_value=71.0 normalized_unit=mM; kcat/Km normalized_value=0.1104225352112676 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=7.84 raw_unit=s^-1; Km raw_value=71 raw_unit=mM; Vmax/Km raw_value=110 raw_unit=s^-1 M^-1

row_label: d-Serine; YMR226C column group (B)

table_label: Table 4. Kinetic parameters of YdfG (A) and YMR226C (B)

substrate: D-serine


column_label: Official ScienceDirect HTML Table 4 row l-3-Hydroxybutyrate gives YMR226C (B) kcat 9.38 s^-1, Km 95 mM, and Vmax/Km 99 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=9.38 normalized_unit=s^-1; Km normalized_value=95.0 normalized_unit=mM; kcat/Km normalized_value=0.09873684210526316 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=9.38 raw_unit=s^-1; Km raw_value=95 raw_unit=mM; Vmax/Km raw_value=99 raw_unit=s^-1 M^-1

row_label: l-3-Hydroxybutyrate; YMR226C column group (B)


column_label: Official ScienceDirect HTML Table 4 row l-Serine gives YMR226C (B) kcat 11.0 s^-1, Km 95 mM, and Vmax/Km 116 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=11.0 normalized_unit=s^-1; Km normalized_value=95.0 normalized_unit=mM; kcat/Km normalized_value=0.11578947368421053 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=11.0 raw_unit=s^-1; Km raw_value=95 raw_unit=mM; Vmax/Km raw_value=116 raw_unit=s^-1 M^-1

row_label: l-Serine; YMR226C column group (B)


column_label: Official ScienceDirect HTML Table 4 row l-allo-Threonine gives YMR226C (B) kcat 43.8 s^-1, Km 3 mM, and Vmax/Km 14,600 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=43.8 normalized_unit=s^-1; Km normalized_value=3.0 normalized_unit=mM; kcat/Km normalized_value=14.6 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=43.8 raw_unit=s^-1; Km raw_value=3 raw_unit=mM; Vmax/Km raw_value=14,600 raw_unit=s^-1 M^-1

row_label: l-allo-Threonine; YMR226C column group (B)


substrate_name: D-Threonine

column_label: Official ScienceDirect HTML Table 4 row d-Threonine gives YMR226C (B) kcat 52.8 s^-1, Km 7 mM, and Vmax/Km 7540 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=52.8 normalized_unit=s^-1; Km normalized_value=7.0 normalized_unit=mM; kcat/Km normalized_value=7.542857142857143 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=52.8 raw_unit=s^-1; Km raw_value=7 raw_unit=mM; Vmax/Km raw_value=7540 raw_unit=s^-1 M^-1

row_label: d-Threonine; YMR226C column group (B)


enzyme_display_name: L-rhamnose 1-dehydrogenase (NADP(+))

organism: Thermoplasma acidophilum

substrate_name: L-Lyxose

enzyme: L-rhamnose 1-dehydrogenase (NADP(+))

substrate: L-Lyxose


substrate_name: L-Mannose

substrate: L-Mannose


assay_conditions_summary: pH 7; 333.15 K; cofactor NADP+

proof_lines:
L-rhamnose
NADP(+)
Thermoplasma acidophilum


substrate_name: L-Rhamnose

substrate: L-Rhamnose


enzyme_display_name: sulfoacetaldehyde reductase (NADPH)

organism: Klebsiella oxytoca

substrate_name: isethionate

smiles: O=S(=O)(O)CCO

enzyme: sulfoacetaldehyde reductase (NADPH)

substrate: isethionate


assay_conditions_summary: pH 10; 295.15 K; cofactor NADP+


organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

substrate_name: NAD (with CHMS as substrate at 25 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table 3 row NAD+ (200) lists Km 20.6 +/- 1.0 uM with CHMS in parentheses; table footnote states Km values are for the compounds shown in parentheses.

raw_value_unit_evidence: Km raw_value=20.6 +/- 1.0 raw_unit=uM for CHMS with NAD+.

row_label: LigC / CHMS Km with NAD+ (200 uM cofactor)

table_label: PMC111406 Table 3, kinetic constants of CHMS dehydrogenases


substrate_name: NADP (with CHMS as substrate at 25 degrees Celsius and pH 8)

column_label: Table 3 row NADP+ (200) lists Km 26.0 +/- 0.5 uM with CHMS in parentheses; table footnote states Km values are for the compounds shown in parentheses.

raw_value_unit_evidence: Km raw_value=26.0 +/- 0.5 raw_unit=uM for CHMS with NADP+.

row_label: LigC / CHMS Km with NADP+ (200 uM cofactor)


enzyme_display_name: L-serine 3-dehydrogenase (NAD+)

organism: Pseudomonas aeruginosa

substrate_name: L-serine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9I5I6 and applied mutation signature S122A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 11; 310.15 K; buffer a 1 ml reaction mixture containing 50 mM diethanolamine; cofactor NAD+

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block S122A, variable substrate row L-Serine; column Km (mM) = 10.6; column kcat (s^-1) = 0.4; column kcat/Km (M^-1 s^-1) = 0.4 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.4 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 0.4 s^(-1). Km: printed Table 1 cell 10.6 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 10.6 mM. kcat/Km: printed Table 1 cell 0.4 x 10^2 M^-1 s^-1, that is 40 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 40 / 1000 = 0.04 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block S122A, variable substrate row L-Serine: Km = 10.6 mM; kcat = 0.4 s^-1; printed kcat/Km = 0.4 x 10^2 M^-1 s^-1.

table_label: Table 1: Kinetic parameters of PA0743 with various substrates (J. Biol. Chem. 2012, 287(3):1874-1883)

enzyme: L-serine 3-dehydrogenase (NAD+)

substrate: L-serine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9I5I6 and applied mutation signature Y219A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block Y219A, variable substrate row L-Serine; column Km (mM) = 11.0; column kcat (s^-1) = 0.8; column kcat/Km (M^-1 s^-1) = 0.7 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.8 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 0.8 s^(-1). Km: printed Table 1 cell 11.0 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 11.0 mM. kcat/Km: printed Table 1 cell 0.7 x 10^2 M^-1 s^-1, that is 70 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 70 / 1000 = 0.07 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Y219A, variable substrate row L-Serine: Km = 11.0 mM; kcat = 0.8 s^-1; printed kcat/Km = 0.7 x 10^2 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9I5I6 and applied mutation signature T96A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block T96A, variable substrate row L-Serine; column Km (mM) = 12.3; column kcat (s^-1) = 1.4; column kcat/Km (M^-1 s^-1) = 0.1 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.4 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 1.4 s^(-1). Km: printed Table 1 cell 12.3 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 12.3 mM. kcat/Km: printed Table 1 cell 0.1 x 10^3 M^-1 s^-1, that is 100 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 100 / 1000 = 0.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block T96A, variable substrate row L-Serine: Km = 12.3 mM; kcat = 1.4 s^-1; printed kcat/Km = 0.1 x 10^3 M^-1 s^-1.


assay_conditions_summary: pH 11; 310.15 K; buffer a reaction mixture (1 ml) containing 50 mM diethanolamine; cofactor NAD+

column_label: Table 1, PA0743 wild type NAD+ row: Km 3.4 ± 0.2 mM; kcat 1.6 ± 0.1 s^-1; printed kcat/Km 0.5 × 10^3 M^-1 s^-1 = 0.5 s^-1 mM^-1. The current quotient 0.4705882352941177 lies in both the uncertainty quotient interval [1.5/3.6, 1.7/3.2] = [0.4166666666666667, 0.53125] and the printed-efficiency interval [0.45, 0.55).

normalized_value_unit_evidence: The printed same-row central cells are kcat=1.6 s^-1 and Km=3.4 mM. Their stored-precision quotient is 1.6 / 3.4 = 0.4705882352941177 s^-1 mM^-1. The independently printed efficiency 0.5 × 10^3 M^-1 s^-1 normalizes separately to 0.5 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=3.4 ± 0.2 raw_unit=mM; kcat raw_value=1.6 ± 0.1 raw_unit=s^-1; kcat/Km printed_raw_value=0.5 × 10^3 raw_unit=M^-1 s^-1

row_label: Wild type / NAD+

table_label: Table 1. Kinetic parameters of PA0743 with various substrates


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9I5I6 and applied mutation signature N175A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block N175A, variable substrate row L-Serine; column Km (mM) = 4.2; column kcat (s^-1) = 2.7; column kcat/Km (M^-1 s^-1) = 0.6 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.7 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 2.7 s^(-1). Km: printed Table 1 cell 4.2 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 4.2 mM. kcat/Km: printed Table 1 cell 0.6 x 10^3 M^-1 s^-1, that is 600 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 600 / 1000 = 0.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block N175A, variable substrate row L-Serine: Km = 4.2 mM; kcat = 2.7 s^-1; printed kcat/Km = 0.6 x 10^3 M^-1 s^-1.


substrate_name: D-glycerate

column_label: Table 1 (Kinetic parameters of PA0743 with various substrates), enzyme block Wild type, variable substrate row DL-Glyceric acid; column Km (mM) = 19.8; column kcat (s^-1) = 5.8; column kcat/Km (M^-1 s^-1) = 0.3 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.8 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 5.8 s^(-1). Km: printed Table 1 cell 19.8 mM; the printed unit is already the canonical unit, so no unit conversion applies and the paper side is 19.8 mM. kcat/Km: printed Table 1 cell 0.3 x 10^3 M^-1 s^-1, that is 300 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 300 / 1000 = 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, enzyme block Wild type, variable substrate row DL-Glyceric acid: Km = 19.8 mM; kcat = 5.8 s^-1; printed kcat/Km = 0.3 x 10^3 M^-1 s^-1.

substrate: D-glycerate


substrate_name: DL-threonine

assay_conditions_summary: pH 11

substrate: DL-threonine


assay_conditions_summary: pH 11; 310.15 K; buffer a reaction mixture (1 ml) containing 50 mM diethanolamine; cofactor NADP+

column_label: Table 1, PA0743 wild type L-serine row: Km 2.5 ± 0.1 mM; kcat 10.4 ± 0.2 s^-1; printed kcat/Km 0.4 × 10^4 M^-1 s^-1 = 4.0 s^-1 mM^-1. The current quotient 4.16 lies in both the uncertainty quotient interval [10.2/2.6, 10.6/2.4] = [3.923076923076923, 4.416666666666667] and the printed-efficiency interval [3.5, 4.5).

normalized_value_unit_evidence: The printed same-row central cells are kcat=10.4 s^-1 and Km=2.5 mM. Their stored-precision quotient is 10.4 / 2.5 = 4.16 s^-1 mM^-1. The independently printed efficiency 0.4 × 10^4 M^-1 s^-1 normalizes separately to 4.0 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=2.5 ± 0.1 raw_unit=mM; kcat raw_value=10.4 ± 0.2 raw_unit=s^-1; kcat/Km printed_raw_value=0.4 × 10^4 raw_unit=M^-1 s^-1

row_label: Wild type / L-serine


substrate_name: methyl 2,2-dimethyl-3-hydroxypropionate

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

normalized_value_unit_evidence: The printed same-row central cells are kcat=11.6 s^-1 and Km=17.4 mM. Their stored-precision quotient is 11.6 / 17.4 = 0.6666666666666667 s^-1 mM^-1. The independently printed efficiency 0.7 × 10^3 M^-1 s^-1 normalizes separately to 0.7 s^-1 mM^-1 and is preserved as printed precision.

raw_value_unit_evidence: Km raw_value=17.4 ± 1.2 raw_unit=mM; kcat raw_value=11.6 ± 0.4 raw_unit=s^-1; kcat/Km printed_raw_value=0.7 × 10^3 raw_unit=M^-1 s^-1

row_label: Wild type / MDHP

substrate: methyl 2,2-dimethyl-3-hydroxypropionate


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

substrate_name: glucose 6-phosphate

proof_lines: The catalytic efficiency with NAD(+) is about 230-fold higher than with NADP(+), indicating that NAD(+) is the physiological electron acceptor.

substrate: glucose 6-phosphate


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


enzyme_display_name: NAD(P)H-dependent D-xylose reductase

organism: Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)

substrate_name: DL-Glyceraldehyde

proof_lines: The enzyme was active with various aldose substrates, such as D-galactose and D-glucose.

enzyme: NAD(P)H-dependent D-xylose reductase

substrate: DL-Glyceraldehyde


substrate_name: D-Galactose

substrate: D-Galactose


enzyme_display_name: sulfoquinovose 1-dehydrogenase

organism: Pseudomonas putida

substrate_name: sulfoquinovose

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: with NADP+ as cosubstrate, in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication

proof_lines: with NAD+ as cosubstrate, in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication

proof_lines: kcat is 33.8 sec(-1) for sulfoquinovose oxidation with NAD(+). kcat is 1.4 sec(-1) for sulfoquinovose oxidation with NADP(+).

enzyme: sulfoquinovose 1-dehydrogenase

substrate: sulfoquinovose


organism: Homo sapiens

substrate_name: 3beta-hydroxy-5beta-cholan-24-oic acid

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

substrate: 3beta-hydroxy-5beta-cholan-24-oic acid


enzyme_display_name: NAD-dependent L-serine dehydrogenase

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

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / L-serine: Km=2.5 mM.

normalized_value_unit_evidence: Km=2.5 mM

raw_value_unit_evidence: Km=2.5 mM

row_label: Table 1 / Wild type / L-serine

enzyme: NAD-dependent L-serine dehydrogenase


substrate_name: NAD

assay_conditions_summary: cofactor NAD+

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / NAD+: Km=3.4 mM.

normalized_value_unit_evidence: Km=3.4 mM

raw_value_unit_evidence: Km=3.4 mM

row_label: Table 1 / Wild type / NAD+

substrate: NAD


enzyme_display_name: 3beta-hydroxysteroid dehydrogenase 2

organism: Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B)

proof_lines: kcat is 1750 min(-1) with 12alpha-hydroxy-3-oxo-5beta-cholan-24-oate as substrate.

enzyme: 3beta-hydroxysteroid dehydrogenase 2


enzyme_display_name: 3beta-hydroxysteroid dehydrogenase 1

proof_lines: kcat is 584 min(-1) with 12alpha-hydroxy-3-oxo-5beta-cholan-24-oate as substrate.

enzyme: 3beta-hydroxysteroid dehydrogenase 1


organism: Pyrobaculum calidifontis

substrate_name: NADP+

assay_conditions_summary: pH 10; 323.15 K; cofactor NADP+

proof_lines: pH 10.0, 50°C, recombinant wild-type enzyme

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 10; 323.15 K; cofactor NAD+

substrate: NAD+


substrate_name: DL-glycerate

substrate: DL-glycerate


enzyme_display_name: L-serine 3-dehydrogenase (NAD(+))

substrate_name: D-Glycerate

assay_conditions_summary: pH 11; 310.15 K; cofactor NAD+

proof_lines:
PA0743
NAD+-dependent L-serine dehydrogenase
l-serine

enzyme: L-serine 3-dehydrogenase (NAD(+))

substrate: D-Glycerate


enzyme_display_name: 2-oxoglutarate reductase

organism: Micrococcus aerogenes

enzyme: 2-oxoglutarate reductase


substrate_name: NADH

assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


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


substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines:
NADPH
coenzyme specificities
Candida intermedia

substrate: NADPH


proof_lines:
NADH
coenzyme specificities
Candida intermedia


organism: Fusobacterium nucleatum

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


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

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / Methyl-DL-serine: Km=2.4 mM; Vmax=17.2 umol/min/mg protein; kcat=9.6 s^-1; kcat/Km=0.4 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km=2.4 mM; Vmax=17.2 umol/min/mg protein; kcat=9.6 s^-1; kcat/Km=4.0 s^-1 mM^-1

row_label: Table 1 / Wild type / Methyl-DL-serine


substrate_name: Glycerate

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

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / DL-glyceric acid: Km=19.8 mM; Vmax=10.4 umol/min/mg protein; kcat=5.8 s^-1; kcat/Km=0.3 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km=19.8 mM; Vmax=10.4 umol/min/mg protein; kcat=5.8 s^-1; kcat/Km=0.3 s^-1 mM^-1

row_label: Table 1 / Wild type / DL-glyceric acid

substrate: Glycerate


substrate_name: L-Serine

row_label: Table 1, enzyme block N175A, variable substrate row L-Serine

substrate: L-Serine


row_label: Table 1, enzyme block S122A, variable substrate row L-Serine


row_label: Table 1, enzyme block T96A, variable substrate row L-Serine


column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / L-serine: Km=2.5 mM; Vmax=18.7 umol/min/mg protein; kcat=10.4 s^-1; kcat/Km=0.4 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km=2.5 mM; Vmax=18.7 umol/min/mg protein; kcat=10.4 s^-1; kcat/Km=4.0 s^-1 mM^-1


row_label: Table 1, enzyme block Y219A, variable substrate row L-Serine


substrate_name: DL-threonine

substrate: DL-threonine


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

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / MDHP: Km=17.4 mM; Vmax=20.9 umol/min/mg protein; kcat=11.6 s^-1; kcat/Km=0.7 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km=17.4 mM; Vmax=20.9 umol/min/mg protein; kcat=11.6 s^-1; kcat/Km=0.7 s^-1 mM^-1

row_label: Table 1 / Wild type / MDHP


column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / NAD+: Km=3.4 mM; Vmax=2.8 umol/min/mg protein; kcat=1.6 s^-1; kcat/Km=0.5 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km=3.4 mM; Vmax=2.8 umol/min/mg protein; kcat=1.6 s^-1; kcat/Km=0.5 s^-1 mM^-1


organism: Eggerthella lenta


enzyme_display_name: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 2

organism: Clostridium scindens (strain JCM 10418 / VPI 12708)

substrate_name: choloyl-CoA (at pH 8.7 and 37 degrees Celsius)

assay_conditions_summary: pH 8.7; cofactor CoA

proof_lines: kcat is 10 min(-1) with choloyl-CoA as substrate. kcat is 12 min(-1) with chenodeoxycholoyl-CoA as substrate. kcat is 11 min(-1) with lithocholoyl-CoA as substrate. kcat is 9.5 min(-1) with deoxycholoyl-CoA as substrate. kcat is 8.3 min(-1)


substrate_name: chenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)

enzyme: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 2


substrate_name: lithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: deoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxochenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxolithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: 3-oxodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate_name: NAD(+) (at pH 8.7 and 37 degrees Celsius)


substrate_name: NADP(+) (at pH 8.7 and 37 degrees Celsius)


enzyme_display_name: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 1/3

proof_lines: kcat is 74 min(-1) with choloyl-CoA as substrate. kcat is 49 min(-1) with chenodeoxycholoyl-CoA as substrate. kcat is 44 min(-1) with lithocholoyl-CoA as substrate. kcat is 52 min(-1) with deoxycholoyl-CoA as substrate. kcat is 33 min(-1) w

substrate: choloyl-CoA (at pH 8.7 and 37 degrees Celsius)


enzyme: 3alpha-hydroxy bile acid-CoA-ester 3-dehydrogenase 1/3

substrate: chenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate: lithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate: deoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate: 3-oxocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate: 3-oxochenodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate: 3-oxolithocholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate: 3-oxodeoxycholoyl-CoA (at pH 8.7 and 37 degrees Celsius)


substrate: NAD(+) (at pH 8.7 and 37 degrees Celsius)


substrate: NADP(+) (at pH 8.7 and 37 degrees Celsius)


organism: Actinomadura kijaniata

substrate_name: dTDP-glucose

proof_lines: kcat is 6.24 sec(-1) for dTDP-glucose as substrate.

substrate: dTDP-glucose


assay_conditions_summary: cofactor NADPH


enzyme_display_name: D-3-phosphoglycerate dehydrogenase

organism: Escherichia coli (strain K12)

proof_lines: kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2-hydroxyglutarate oxidation. kcat is 0.25

enzyme: D-3-phosphoglycerate dehydrogenase


proof_lines: kcat is 4.5 min(-1) for 3-phosphoglycerate oxidation. kcat is 10.6 min(-1) for oxaloacetate reduction. kcat is 4.7 min(-1) for 2-oxoglutarate reduction.


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


enzyme_display_name: 3alpha-hydroxysteroid dehydrogenase

organism: Mediterraneibacter gnavus (strain ATCC 29149 / DSM 114966 / JCM 6515 / VPI C7-9)

substrate_name: deoxycholate

proof_lines: kcat is 99.3 min(-1) with deoxycholate as substrate.

enzyme: 3alpha-hydroxysteroid dehydrogenase

substrate: deoxycholate


enzyme_display_name: 3beta-hydroxysteroid dehydrogenase

proof_lines: kcat is 9430 min(-1) with 12alpha-hydroxy-3-oxo-5beta-cholan-24-oate as substrate.

enzyme: 3beta-hydroxysteroid dehydrogenase


enzyme_display_name: D-3-phosphoglycerate dehydrogenase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

column_label: Table 3. Kinetic properties of the alpha-ketoglutarate reductase activity of Ser3 and Ser33, Table 3 / Ser3: Km=49 uM.

raw_value_unit_evidence: Km=49 uM

row_label: Table 3 / Ser3

enzyme: D-3-phosphoglycerate dehydrogenase 1


enzyme_display_name: D-3-phosphoglycerate dehydrogenase 2

column_label: Table 3. Kinetic properties of the alpha-ketoglutarate reductase activity of Ser3 and Ser33, Table 3 / Ser33: Km=54 uM.

raw_value_unit_evidence: Km=54 uM

row_label: Table 3 / Ser33

enzyme: D-3-phosphoglycerate dehydrogenase 2


enzyme_display_name: (R)-2-hydroxyglutarate dehydrogenase

organism: Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4)

enzyme: (R)-2-hydroxyglutarate dehydrogenase


enzyme_display_name: 3alpha-hydroxybile acid CoA 3-dehydrogenase

organism: [Clostridium] scindens

substrate_name: lithocholoyl-CoA

assay_conditions_summary: pH 8.7; 310.15 K; cofactor CoA

column_label: Table II; row BaiA1 / LC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 44, KM 22, and kcat/KM 2.000.

raw_value_unit_evidence: Table II BaiA1 / LC-CoA: kcat = 44 min^-1; KM = 22 uM; kcat/KM = 2.000 uM^-1 min^-1

row_label: BaiA1 / LC-CoA

table_label: Table II

substrate: lithocholoyl-CoA


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P19337 and applied mutation signature E42A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NAD+

column_label: Table IV; row BaiA2_E42A / NAD+; columns BaiA2_E42A kcat, KM, kcat/KM report kcat 19, KM 17, and kcat/KM 1.11.

raw_value_unit_evidence: Table IV BaiA2_E42A / NAD+: kcat = 19 min^-1; KM = 17 uM; kcat/KM = 1.11 uM^-1 min^-1

row_label: BaiA2_E42A / NAD+

table_label: Table IV

enzyme: 3alpha-hydroxybile acid CoA 3-dehydrogenase

substrate: NAD+


column_label: Table IV; row BaiA1 / NAD+; columns BaiA1 kcat, KM, kcat/KM report kcat 18, KM 17, and kcat/KM 1.06.

raw_value_unit_evidence: Table IV BaiA1 / NAD+: kcat = 18 min^-1; KM = 17 uM; kcat/KM = 1.06 uM^-1 min^-1

row_label: BaiA1 / NAD+


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E42A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NADP+

substrate: NADP+


column_label: Table IV; row BaiA1 / NADP+; columns BaiA1 kcat, KM, kcat/KM report kcat 6.8, KM 883, and kcat/KM 0.008.

raw_value_unit_evidence: Table IV BaiA1 / NADP+: kcat = 6.8 min^-1; KM = 883 uM; kcat/KM = 0.008 uM^-1 min^-1

row_label: BaiA1 / NADP+


substrate_name: taurocholic acid

column_label: Table II; row BaiA1 / TCA; columns BaiA1 kcat, KM, kcat/KM report kcat 24, KM 329, and kcat/KM 0.073.

raw_value_unit_evidence: Table II BaiA1 / TCA: kcat = 24 min^-1; KM = 329 uM; kcat/KM = 0.073 uM^-1 min^-1

row_label: BaiA1 / TCA

substrate: taurocholic acid


enzyme_display_name: eugenol synthase

organism: Ocimum basilicum

substrate_name: coniferyl acetate

enzyme: eugenol synthase

substrate: coniferyl acetate


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH

column_label: Package PDF/text Table 2 row ObaIEGS, substrate Coniferyl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 0.7 mM; kcat 0.23 min^-1; kcat/Km 0.33 mM^-1 min^-1; paper exact kcat/Km=0.33 mM^-1 min^-1

row_label: ObaIEGS / Coniferyl acetate

table_label: Table 2, Values of kinetic parameters for four recombinant EGS


column_label: Table II; row BaiA1 / 3-oxo-CDC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 24, KM 3.3, and kcat/KM 7.230.

raw_value_unit_evidence: Table II BaiA1 / 3-oxo-CDC-CoA: kcat = 24 min^-1; KM = 3.3 uM; kcat/KM = 7.230 uM^-1 min^-1

row_label: BaiA1 / 3-oxo-CDC-CoA


column_label: Table II; row BaiA1 / 3-oxo-C-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 33, KM 9.1, and kcat/KM 3.626.

raw_value_unit_evidence: Table II BaiA1 / 3-oxo-C-CoA: kcat = 33 min^-1; KM = 9.1 uM; kcat/KM = 3.626 uM^-1 min^-1

row_label: BaiA1 / 3-oxo-C-CoA


column_label: Table II; row BaiA1 / 3-oxo-DC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 44, KM 5.6, and kcat/KM 7.860.

raw_value_unit_evidence: Table II BaiA1 / 3-oxo-DC-CoA: kcat = 44 min^-1; KM = 5.6 uM; kcat/KM = 7.860 uM^-1 min^-1

row_label: BaiA1 / 3-oxo-DC-CoA


column_label: Table II; row BaiA1 / 3-oxo-LC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 42, KM 8.3, and kcat/KM 5.060.

raw_value_unit_evidence: Table II BaiA1 / 3-oxo-LC-CoA: kcat = 42 min^-1; KM = 8.3 uM; kcat/KM = 5.060 uM^-1 min^-1

row_label: BaiA1 / 3-oxo-LC-CoA


substrate_name: chenodeoxycholic acid

column_label: Table II, CDCA row under BaiA1 columns reports kcat 15, KM 555, and kcat/KM 0.027.

raw_value_unit_evidence: Table II BaiA1 row CDCA: kcat = 15 min^-1; KM = 555 uM; kcat/KM = 0.027 uM^-1 min^-1

row_label: BaiA1 / CDCA

substrate: chenodeoxycholic acid


substrate_name: chenodeoxycholoyl-CoA

column_label: Table II; row BaiA1 / CDC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 49, KM 53, and kcat/KM 0.925.

raw_value_unit_evidence: Table II BaiA1 / CDC-CoA: kcat = 49 min^-1; KM = 53 uM; kcat/KM = 0.925 uM^-1 min^-1

row_label: BaiA1 / CDC-CoA

substrate: chenodeoxycholoyl-CoA


substrate_name: cholic acid

column_label: Table II, CA row under BaiA1 columns reports kcat 16, KM 1158, and kcat/KM 0.014.

raw_value_unit_evidence: Table II BaiA1 row CA: kcat = 16 min^-1; KM = 1158 uM; kcat/KM = 0.014 uM^-1 min^-1

row_label: BaiA1 / CA

substrate: cholic acid


substrate_name: choloyl-CoA

column_label: Table II, C-CoA row under BaiA1 columns reports kcat 74, KM 106, and kcat/KM 0.698.

raw_value_unit_evidence: Table II BaiA1 row C-CoA: kcat = 74 min^-1; KM = 106 uM; kcat/KM = 0.698 uM^-1 min^-1

row_label: BaiA1 / C-CoA

substrate: choloyl-CoA


substrate_name: deoxycholoyl-CoA

column_label: Table II; row BaiA1 / DC-CoA; columns BaiA1 kcat, KM, kcat/KM report kcat 52, KM 16, and kcat/KM 3.250.

raw_value_unit_evidence: Table II BaiA1 / DC-CoA: kcat = 52 min^-1; KM = 16 uM; kcat/KM = 3.250 uM^-1 min^-1

row_label: BaiA1 / DC-CoA

substrate: deoxycholoyl-CoA


substrate_name: glycocholic acid

column_label: Table II; row BaiA1 / GCA; columns BaiA1 kcat, KM, kcat/KM report kcat 25, KM 383, and kcat/KM 0.065.

raw_value_unit_evidence: Table II BaiA1 / GCA: kcat = 25 min^-1; KM = 383 uM; kcat/KM = 0.065 uM^-1 min^-1

row_label: BaiA1 / GCA

substrate: glycocholic acid


organism: Ocimum tenuiflorum

substrate_name: 4-coumaryl acetate

column_label: Package PDF/text Table 2 row OtIEGS, substrate Coumaryl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 1.7 mM; kcat 0.8 min^-1; kcat/Km 0.47 mM^-1 min^-1; paper exact kcat/Km=0.47 mM^-1 min^-1

row_label: OtIEGS / Coumaryl acetate

substrate: 4-coumaryl acetate


column_label: Package PDF/text Table 2 row OtIEGS, substrate Coniferyl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 1.17 mM; kcat 1.68 min^-1; kcat/Km 1.44 mM^-1 min^-1; paper exact kcat/Km=1.44 mM^-1 min^-1

row_label: OtIEGS / Coniferyl acetate


organism: Ocimum gratissimum

column_label: Package PDF/text Table 2 row OgIEGS, substrate Coumaryl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 1.25 mM; kcat 0.2017 min^-1; kcat/Km 0.16 mM^-1 min^-1; paper exact kcat/Km=0.16 mM^-1 min^-1

row_label: OgIEGS / Coumaryl acetate


column_label: Package PDF/text Table 2 row OgIEGS, substrate Coniferyl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 0.5 mM; kcat 0.68 min^-1; kcat/Km 1.36 mM^-1 min^-1; paper exact kcat/Km=1.36 mM^-1 min^-1

row_label: OgIEGS / Coniferyl acetate


organism: Ocimum kilimandscharicum

column_label: Package PDF/text Table 2 row OkEGS, substrate Coumaryl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 0.55 mM; kcat 0.63 min^-1; kcat/Km 1.15 mM^-1 min^-1; paper exact kcat/Km=1.15 mM^-1 min^-1

row_label: OkEGS / Coumaryl acetate


column_label: Package PDF/text Table 2 row OkEGS, substrate Coniferyl acetate, columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Km 0.41 mM; kcat 0.18 min^-1; kcat/Km 0.44 mM^-1 min^-1; paper exact kcat/Km=0.44 mM^-1 min^-1

row_label: OkEGS / Coniferyl acetate


enzyme_display_name: isoeugenol synthase

organism: Pimpinella anisum

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

column_label: Table II, AIS1 row, Coumaryl acetate: Km column 134.9 +/- 36.4 uM; kcat column 0.07 +/- 0.01 s^-1; kcat/Km column 0.52 s^-1 mM^-1; footnote a = averages of three independent experiments +/- SE.

row_label: AIS1 / Coumaryl acetate

table_label: Table II - Kinetic parameters of AIS1 and AIMT1

enzyme: isoeugenol synthase


column_label: Table II, AIS1 row, Coniferyl acetate: Km column 229.9 +/- 46.2 uM; kcat column 1.02 +/- 0.17 s^-1; kcat/Km column 4.44 s^-1 mM^-1; footnote a = averages of three independent experiments +/- SE.

row_label: AIS1 / Coniferyl acetate


enzyme_display_name: Chanoclavine-I dehydrogenase easD

organism: Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371)

substrate_name: chanoclavine-I

column_label: The abstract reports Km values for chanoclavine-I and NAD+ were 0.09 and 0.36 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.09 mM raw_unit=mM

row_label: Prose segment: chanoclavine-I Km

table_label: PubMed PMID 22403186 abstract

enzyme: Chanoclavine-I dehydrogenase easD

substrate: chanoclavine-I


raw_value_unit_evidence: Km raw_value=0.36 mM raw_unit=mM

row_label: Prose segment: NAD+ Km


organism: Daucus carota subsp. sativus

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: chanoclavine-I dehydrogenase

organism: Aspergillus fumigatus

enzyme: chanoclavine-I dehydrogenase


substrate_name: Chanoclavine-I

substrate: Chanoclavine-I


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Staphylococcus aureus

substrate_name: D-Ribulose 5-phosphate; NADPH; H+

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

substrate: D-Ribulose 5-phosphate; NADPH; H+


substrate_name: D-Ribulose 5-phosphate

substrate: D-Ribulose 5-phosphate


assay_conditions_summary: pH 7.2; 295.15 K; cofactor NADPH


enzyme_display_name: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Bcs1

organism: Haemophilus influenzae

substrate_name: D-ribulose 5-phosphate

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

proof_lines: kcat is 22 sec(-1) for the reductase reaction. kcat is 13 sec(-1) for the cytidyltransferase reaction.

substrate: D-ribulose 5-phosphate


enzyme: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Bcs1


substrate_name: D-ribitol 5-phosphate (for the cytidylyltransferase reaction)

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


substrate_name: CTP

substrate: CTP


organism: Chromobacterium violaceum


substrate_name: UDP-alpha-D-glucuronate

column_label: pmc3050068_jats.xml table-wrap T3: row Km for the UDP-sugar / column C. violaceum WlbA with UDP-GlcA = 0.20 +/- 0.02; row kcat = 0.00015 +/- 0.00001; row kcat/Km UDP-linked sugar = 0.75

raw_value_unit_evidence: Table 3 column C. violaceum WlbA with UDP-GlcA: Km 0.20 +/- 0.02 mM; kcat 0.00015 +/- 0.00001 s^-1; kcat/Km 0.75 M^-1 s^-1

row_label: C. violaceum WlbA with UDP-GlcA; rows Km for the UDP-sugar, kcat, kcat/Km UDP-linked sugar

table_label: Table 3 Kinetic Parameters

substrate: UDP-alpha-D-glucuronate


enzyme_display_name: tetrachlorobenzoquinone reductase

organism: Sphingobium chlorophenolicum

assay_conditions_summary: pH 7.6; cofactor NADPH

proof_lines: kcat is 20.1 sec(-1) for NADH as substrate (with 90 uM cytochrome c). kcat is 14.1 sec(-1) for 2,6-dichloroindophenol (DCIP) as substrate (with 100 uM NADH). kcat is 9.1 sec(-1) for cytochrome c as substrate (with 100 uM NADH). kcat is 3.7

enzyme: tetrachlorobenzoquinone reductase


substrate_name: NADH

assay_conditions_summary: pH 7.6; cofactor NADH

substrate: NADH


enzyme_display_name: D-threitol dehydrogenase

organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: D-threitol

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

proof_lines: kcat is 6.97 sec(-1) with D-threitol as substrate. kcat is 0.71 sec(-1) with D-threose as substrate. kcat is 7.32 sec(-1) with D-erythrulose as substrate.

enzyme: D-threitol dehydrogenase

substrate: D-threitol


substrate_name: D-threose

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

substrate: D-threose


substrate_name: D-erythrulose

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

substrate: D-erythrulose


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

substrate_name: UDP-GlcNAcA

column_label: Table 3 reports the P. aeruginosa row with Km (mM) UDP-GlcNAcA = 0.25 +/- 0.01 mM.

raw_value_unit_evidence: Km raw_value=0.25 +/- 0.01 raw_unit=mM

row_label: P. aeruginosa WlbA enzyme

table_label: PMID 20690587 Table 3, Kinetic Parameters

substrate: UDP-GlcNAcA


column_label: Table 3 reports the P. aeruginosa row with Km (mM) alpha-ketoglutarate = 1.35 +/- 0.10 mM.

raw_value_unit_evidence: Km raw_value=1.35 +/- 0.10 raw_unit=mM


organism: Sphingomonas sp.

assay_conditions_summary: pH 8

proof_lines: kcat is 51.8 min(-1) with 2-dehydro-3-deoxy-L-rhamnonate as substrate. kcat is 11 min(-1) with 2-dehydro-3-deoxy-L-lyxonate as substrate. kcat is 0.72 min(-1) with 2-dehydro-3-deoxy-L-mannonate as substrate.


enzyme_display_name: Ribulose-5-phosphate reductase

organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

enzyme: Ribulose-5-phosphate reductase


enzyme_display_name: D-altritol 5-dehydrogenase

organism: Agrobacterium fabrum

substrate_name: D-altritol

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

assay_conditions_summary: pH 9

enzyme: D-altritol 5-dehydrogenase

substrate: D-altritol


organism: Cereibacter sphaeroides

substrate_name: galactitol

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

substrate: galactitol


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


smiles: CCCCC(CO)O

assay_conditions_summary: pH 6.5; cofactor NAD+

column_label: Official article text lists apparent Km values and gives 1,2-hexandiol as 0-2 mM.

raw_value_unit_evidence: Km raw_value=0-2 raw_unit=mM

row_label: Rhodobacter sphaeroides D galactitol dehydrogenase with 1,2-hexanediol (paper spelling: 1,2-hexandiol)

table_label: Microbiology Society official article abstract/full-text summary, PMID 7551050


substrate_name: dihydroxyacetone

smiles: CC(=O)CO

substrate: dihydroxyacetone


substrate_name: acetoin

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

substrate: acetoin


substrate_name: L-erythrulose

substrate: L-erythrulose


enzyme_display_name: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Acs1

substrate_name: D-ribulose 5-phosphate (in the presence of 50 uM CTP)

column_label: HTML prose names Km for ribulose 5-phosphate under 50 uM CTP condition

raw_value_unit_evidence: 50 uM with 50 uM CTP

row_label: CTP addition decreases ribulose 5-phosphate Km from 400 to 50 uM

table_label: PMC HTML Results section: Characterization and kinetic properties of Acs1 (prose)


substrate_name: NADPH

enzyme: Bifunctional ribulose 5-phosphate reductase/CDP-ribitol pyrophosphorylase Acs1

substrate: NADPH


assay_conditions_summary: cofactor NADP+

column_label: HTML prose names Km for ribitol 5-phosphate under pyrophosphorylase activity

raw_value_unit_evidence: 37 uM

row_label: Km for ribitol 5-phosphate reported as 37 uM

substrate: D-ribitol 5-phosphate (for the cytidylyltransferase reaction)


column_label: HTML prose names Km for CTP; UTP replacement reported inactive

row_label: Km for CTP reported as 150 uM


smiles: C(CCO)CC(CO)O

proof_lines: Also (S)-1,2,6-hexanetriol was oxidized by GDH


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

proof_lines: The diketone 2,3-hexanedione was only reduced


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


smiles: CCC(=O)CO

proof_lines: Reduction of hydroxyacetone or 1-hydroxy-2-butanone


smiles: CCC(CO)O

proof_lines: The oxidation of 1,2-butanediol occurred highly specific


smiles: CC(CO)O


substrate_name: Hydroxyacetone

substrate: Hydroxyacetone


substrate_name: D-Arabinose 5-phosphate

column_label: PDF page 4 Table 1 lists D-arabinose 5-phosphate under reductase: Km 3000 +/- 570 uM; kcat 2.3 +/- 0.3 s^-1; kcat/Km 0.0077 x10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=2.3 normalized_unit=s^-1; Km normalized_value=3.0 normalized_unit=mM; kcat/Km normalized_value=0.7666666666666666 normalized_unit=s^-1*mM^-1 from the same table kcat and Km cells; printed table specificity constant is 0.0077 x10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1 D-arabinose 5-phosphate cells: Km raw_value=3000 +/- 570 raw_unit=uM; kcat raw_value=2.3 +/- 0.3 raw_unit=s^-1; kcat/Km raw_value=0.0077 raw_unit=x10^5 M^-1 s^-1.

row_label: (1) reductase / D-arabinose 5-phosphate

table_label: Table 1: Steady State Kinetic Parameters Describing Substrate Specificity of Reductase and Cytidylyltransferase Activities of Bcs1

substrate: D-Arabinose 5-phosphate


substrate_name: D-Ribose 5-phosphate

column_label: PDF page 4 Table 1 lists D-ribose 5-phosphate under reductase: Km 2200 +/- 280 uM; kcat 4.1 +/- 0.3 s^-1; kcat/Km 0.019 x10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=4.1 normalized_unit=s^-1; Km normalized_value=2.2 normalized_unit=mM; kcat/Km normalized_value=1.8636363636363633 normalized_unit=s^-1*mM^-1 from the same table kcat and Km cells; printed table specificity constant is 0.019 x10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1 D-ribose 5-phosphate cells: Km raw_value=2200 +/- 280 raw_unit=uM; kcat raw_value=4.1 +/- 0.3 raw_unit=s^-1; kcat/Km raw_value=0.019 raw_unit=x10^5 M^-1 s^-1.

row_label: (1) reductase / D-ribose 5-phosphate

substrate: D-Ribose 5-phosphate


substrate_name: D-Ribulose

column_label: PDF page 4 Table 1 lists D-ribulose under reductase: Km 1100 +/- 180 uM; kcat 3.6 +/- 0.3 s^-1; kcat/Km 0.033 x10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=3.6 normalized_unit=s^-1; Km normalized_value=1.1 normalized_unit=mM; kcat/Km normalized_value=3.2727272727272725 normalized_unit=s^-1*mM^-1 from the same table kcat and Km cells; printed table specificity constant is 0.033 x10^5 M^-1 s^-1.

raw_value_unit_evidence: Table 1 D-ribulose cells: Km raw_value=1100 +/- 180 raw_unit=uM; kcat raw_value=3.6 +/- 0.3 raw_unit=s^-1; kcat/Km raw_value=0.033 raw_unit=x10^5 M^-1 s^-1.

row_label: (1) reductase / D-ribulose

substrate: D-Ribulose


substrate_name: D-Ribulose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K386A to reconstruct the assayed variant sequence.

substrate: D-Ribulose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R18A to reconstruct the assayed variant sequence.


column_label: Table 1; reductase block; row D-ribulose 5-phosphate; columns Kma, kcata, kcat/Km.

normalized_value_unit_evidence: Km paper=0.076 mM; kcat paper=22 s^-1; kcat/Km paper=290 s^-1 mM^-1; export kcat=26.0 and kcat/Km=342.10526315789474.

row_label: D-ribulose 5-phosphate

table_label: Table 1. Steady State Kinetic Parameters Describing Substrate Specificity of Reductase and Cytidylyltransferase Activities of Bcs1


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH


column_label: Table 1; reductase block; row NADPH; columns Kma, kcata, kcat/Km.

normalized_value_unit_evidence: Km paper=0.044 mM; kcat paper=22 s^-1; kcat/Km paper=500 s^-1 mM^-1; export kcat=26.0 and kcat/Km=590.909090909091.

row_label: NADPH


substrate_name: D-Xylulose 5-phosphate

substrate: D-Xylulose 5-phosphate


assay_conditions_summary: pH 7.6; 295.15 K; cofactor NADH

column_label: Table 1 row DCIP (with 100 uM NADH), PcpD column reports kcat 14.1+/-0.6 s^-1, Km 38.3+/-2.5 uM, and kcat/Km (3.68+/-0.15)x10^5 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=14.1 normalized_unit=s^-1; Km normalized_value=0.0383 normalized_unit=mM; kcat/Km normalized_value=368.0 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=14.1+/-0.6 raw_unit=s^-1; Km raw_value=38.3+/-2.5 raw_unit=uM; kcat/Km raw_value=(3.68+/-0.15)x10^5 raw_unit=M^-1 s^-1

row_label: DCIP (with 100 uM NADH), PcpD column

table_label: PMC3683723 Table 1


substrate_name: NADH

column_label: Table 1, NADH (with 90 uM cytochrome c) row, full-length PcpD kcat, KM, and kcat/KM cells; the adjacent PcpD-FeS construct is excluded.

row_label: NADH (with 90 uM cytochrome c) / PcpD

table_label: Table 1. Kinetic parameters for reactions of PcpD with TCBQ, DCIP, and cytochrome c

substrate: NADH


assay_conditions_summary: pH 7.6; 295.15 K; cofactor NADPH

column_label: Table 1 row NADPH (with 90 uM cytochrome c), PcpD column reports kcat 3.7+/-0.3 s^-1, Km 1.21 mM, and kcat/Km (3.1+/-0.1)x10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat normalized_value=3.7 normalized_unit=s^-1; Km normalized_value=1.21 normalized_unit=mM; kcat/Km normalized_value=3.1 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=3.7+/-0.3 raw_unit=s^-1; Km raw_value=1.21 raw_unit=mM; kcat/Km raw_value=(3.1+/-0.1)x10^3 raw_unit=M^-1 s^-1


organism: Methanobrevibacter millerae

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH


substrate_name: sulfopyruvate

substrate: sulfopyruvate


enzyme_display_name: aldose 1-dehydrogenase [NAD(P)(+)]

organism: Saccharolobus solfataricus

substrate_name: beta-D-glucose

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+

column_label: Table II row D-Glucose / NAD+ gives Km 1.50, kcat 74.9, kcat/Km 49.9.

row_label: D-Glucose / NAD+

table_label: TABLE II. Kinetic parameters of glucose dehydrogenase from S. solfataricus at 70 C

enzyme: aldose 1-dehydrogenase [NAD(P)(+)]

substrate: beta-D-glucose


substrate_name: D-galactose

column_label: Table II row D-Galactose / NAD+ gives Km 0.57, kcat 61.3, kcat/Km 107.5.

row_label: D-Galactose / NAD+

substrate: D-galactose


organism: Escherichia coli (strain K12)

substrate_name: UDP-ManNAc (in the presence of 1 mM N-acetylglucosamine-1-P)


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: Glucose/galactose 1-dehydrogenase

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

substrate_name: D-glucose

enzyme: Glucose/galactose 1-dehydrogenase

substrate: D-glucose


substrate_name: NADP(+)

column_label: The Wiley full text states that kinetic analysis resulted in apparent Km values of 10 (+/- 1) mM for glucose at 5 mM NADP+ and 1.12 (+/- 0.2) mM for NADP+ at 50 mM glucose.

raw_value_unit_evidence: Km raw_value=1.12 raw_unit=mM

row_label: recombinant Picrophilus torridus GdhA / NADP+

table_label: Wiley full text PMID 15691337 GdhA kinetic analysis prose

substrate: NADP(+)


enzyme_display_name: glucose-6-phosphate 3-dehydrogenase

organism: Bacillus subtilis

substrate_name: D-glucose 6-phosphate

enzyme: glucose-6-phosphate 3-dehydrogenase

substrate: D-glucose 6-phosphate


substrate_name: NAD+

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Pseudomonas putida

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

column_label: Table 1 columns NAD, KM (uM), and kcat (s^-1); same row provides the primary values used to derive kcat/KM.

row_label: NAD

table_label: Table 1: Kinetic parameters obtained for PputG6PDH-1


substrate_name: NADP+

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

column_label: Table 1 columns NADP, KM (uM), and kcat (s^-1); same row provides the primary values used to derive kcat/KM.

row_label: NADP

substrate: NADP+


enzyme_display_name: UDP-N-acetylglucosamine 3-dehydrogenase

organism: Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)

substrate_name: UDP-GlcNAc

enzyme: UDP-N-acetylglucosamine 3-dehydrogenase

substrate: UDP-GlcNAc


enzyme_display_name: L-arabinose 1-dehydrogenase (NAD(P)(+))

organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

enzyme: L-arabinose 1-dehydrogenase (NAD(P)(+))


organism: Methanococcus maripaludis

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Rhodococcus sp. AD45

assay_conditions_summary: pH 10; cofactor NAD+

column_label: Primary-paper PMC Results prose reports HGMB oxidation followed Michaelis-Menten kinetics and the Km for NAD+ was 0.07 mM at 7.5 mM HGMB.

raw_value_unit_evidence: NAD+ Km 0.07 mM at 7.5 mM HGMB

row_label: NAD+ substrate Km sentence

table_label: Results prose: Purification of the HGMB-dependent dehydrogenase


column_label: Primary-paper PMC Results prose reports HGMB oxidation followed Michaelis-Menten kinetics and the Km for HGMB was 1.4 mM.

raw_value_unit_evidence: HGMB Km 1.4 mM

row_label: HGMB substrate Km sentence


organism: Sulfobacillus thermosulfidooxidans

assay_conditions_summary: pH 9.5; cofactor NAD+

proof_lines:
pH 9.5, 50°C
at pH 9.5 and 50°C


column_label: Abstract states the K m and V max values for L-KDR were 2.0 mM and 12.8 U/mg, respectively.

raw_value_unit_evidence: Km raw_value=2.0 mM raw_unit=mM

row_label: Sulth_3557 KDRDH / L-KDR

table_label: PubMed XML abstract


organism: Haloferax volcanii

assay_conditions_summary: pH 8; cofactor NAD+


assay_conditions_summary: pH 8


enzyme_display_name: Ribulose-5-phosphate reductase 2

organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: Ribulose-5-phosphate reductase 2

substrate: NADPH


substrate_name: ribulose 5-phosphate

substrate: ribulose 5-phosphate


enzyme_display_name: 2-oxoglutarate reductase

organism: Homo sapiens

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

assay_conditions_summary: pH 7.6; 310.15 K; cofactor NADH

column_label: Table 1, reaction column 'α-ketoglutarate → 2-hydroxyglutarate': row 'Kcat (1/min)' cell = 4.7 (printed as '4.7 ± ...'), row 'Km, α-ketoglutarate (mM)' cell = 10.1. Table 1 prints no kcat/Km column; the kcat/Km entry is the quotient of those two cells, 4.7 (1/min) / 10.1 (mM).

normalized_value_unit_evidence: kcat raw 4.7 1/min normalizes to 0.07833333333333334 s^-1 (divide by 60); km raw 10.1 mM normalizes to 10.1 mM; kcat/Km = 0.07833333333333334 s^-1 / 10.1 mM = 0.007755775577557756 s^-1 mM^-1 (quotient of the two printed Table 1 cells; the paper prints no kcat/Km column).

raw_value_unit_evidence: Table 1; reaction column α-ketoglutarate → 2-hydroxyglutarate; column 'Kcat (1/min)'; raw value 4.7 1/min | Table 1; reaction column α-ketoglutarate → 2-hydroxyglutarate; column 'Km, α-ketoglutarate (mM)'; raw value 10.1 mM

row_label: α-ketoglutarate → 2-hydroxyglutarate | Km, α-ketoglutarate (mM)

table_label: Table 1. Michaelis-Menten Parameters of the Different Reactions Catalyzed by PHGDH, Compared to Intracellular Concentrations of the Corresponding Substrates and Products in Different Cell Lines.

enzyme: 2-oxoglutarate reductase


proof_lines:
PHGDH
NADH-dependent AKG reduction
high-affinity NAD(H) binding


enzyme_display_name: Ribulose-5-phosphate reductase 1

column_label: Table 2 lists TarIJ reductase NADPH Km (uM) as 6.74 +/- 1.64, which normalizes to 0.00674 mM and matches the exported NADPH Km.

raw_value_unit_evidence: Km raw_value=6.74 +/- 1.64 raw_unit=uM

row_label: TarIJ reductase / NADPH

table_label: Table 2: Summary of Kinetic Constants

enzyme: Ribulose-5-phosphate reductase 1


substrate_name: D-ribulose 5-phosphate

column_label: Table 2 lists TarIJ reductase ribulose-5-P Km (uM) as 28.5 +/- 13.1, which normalizes to 0.0285 mM and matches the exported D-ribulose 5-phosphate Km.

raw_value_unit_evidence: Km raw_value=28.5 +/- 13.1 raw_unit=uM

row_label: TarIJ reductase / ribulose-5-P

substrate: D-ribulose 5-phosphate


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Yamadazyma tenuis

substrate_name: D-Xylose

assay_conditions_summary: pH 6; 298.15 K; cofactor NADH

proof_lines:
BRENDA EC 1.1.1.307 entry
Yamadazyma tenuis CBS 4435
D-xylose

enzyme: D-xylose reductase [NAD(P)H]

substrate: D-Xylose


enzyme_display_name: D-erythronate dehydrogenase

organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

proof_lines: kcat is 19 sec(-1) with NAD(+) as cosubstrate. kcat is 3.0 sec(-1) with NADP(+) as cosubstrate.

enzyme: D-erythronate dehydrogenase


enzyme_display_name: 4-phospho-D-threonate 3-dehydrogenase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: 4-hydroxy-L-threonine 4-phosphate

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

enzyme: 4-phospho-D-threonate 3-dehydrogenase

substrate: 4-hydroxy-L-threonine 4-phosphate


enzyme_display_name: 2-alkyl-3-oxoalkanoate reductase

organism: Stenotrophomonas maltophilia (strain K279a)

substrate_name: NADP

proof_lines: kcat is 122 min(-1) for syn-2-octyl-3-hydroxydodecanoic acid as substrate. kcat is 85 min(-1) for syn-2-decyl-3-hydroxytetradecanoic acid as substrate. kcat is 79 min(-1) for (2R,3S)-2-hexyl-3-hydroxydecanoic acid as substrate. kcat is 72 m

enzyme: 2-alkyl-3-oxoalkanoate reductase

substrate: NADP


substrate_name: (2R,3S)-2-hexyl-3-hydroxydecanoic acid

substrate: (2R,3S)-2-hexyl-3-hydroxydecanoic acid


enzyme_display_name: L-galactonate 5-dehydrogenase

organism: Phocaeicola vulgatus

substrate_name: L-gluconate

enzyme: L-galactonate 5-dehydrogenase

substrate: L-gluconate


substrate_name: D-tagaturonate

substrate: D-tagaturonate


substrate_name: L-fuconate

substrate: L-fuconate


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

substrate_name: NAD(+)

proof_lines: kcat is 1.9 sec(-1) with NAD(+) as cosubstrate. kcat is 0.88 sec(-1) with NADP(+) as cosubstrate.

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


enzyme_display_name: L-threonate dehydrogenase

organism: Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)

assay_conditions_summary: cofactor NAD+

column_label: Table 1, Q6CZ26 (PaLtnD), l-Threonate, NAD+ row reports K_M 0.13 +/- 0.007.

row_label: Q6CZ26 (PaLtnD), l-Threonate, NAD+

table_label: Table 1

enzyme: L-threonate dehydrogenase


assay_conditions_summary: cofactor NADP+

column_label: Table 1, Q6CZ26 (PaLtnD), l-Threonate, NADP+ row reports K_M 0.97 +/- 0.1.

row_label: Q6CZ26 (PaLtnD), l-Threonate, NADP+


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

proof_lines: kcat is 28 sec(-1) with NAD(+) as cosubstrate. kcat is 3.5 sec(-1) with NADP(+) as cosubstrate.


column_label: Table 1, Q0KBC7 (ReLtnD), l-Threonate, NAD+ row reports K_M 0.35 +/- 0.04.

row_label: Q0KBC7 (ReLtnD), l-Threonate, NAD+


column_label: Table 1, Q0KBC7 (ReLtnD), l-Threonate, NADP+ row reports K_M 0.30 +/- 0.04.

row_label: Q0KBC7 (ReLtnD), l-Threonate, NADP+


proof_lines: kcat is 9.7 sec(-1) with NAD(+) as cosubstrate. kcat is 2.9 sec(-1) with NADP(+) as cosubstrate.


enzyme_display_name: D-erythronate 2-dehydrogenase

organism: Cupriavidus necator

substrate_name: D-erythronate

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

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
cosubstrate NADP+, pH 8.0, 25°C
cosubstrate NAD+, pH 8.0, 25°C

enzyme: D-erythronate 2-dehydrogenase

substrate: D-erythronate


enzyme_display_name: noscapine synthase

organism: Papaver somniferum

substrate_name: narcotine hemiacetal

proof_lines:
pH 8.0, 30°C, cofactor NAD+
pH 8.0, 30°C, cofactor NADP+
cofactor NAD+, pH 8.0, 30°C

enzyme: noscapine synthase

substrate: narcotine hemiacetal


enzyme_display_name: L-threonate 2-dehydrogenase

organism: Pectobacterium atrosepticum

substrate_name: L-threonate

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

enzyme: L-threonate 2-dehydrogenase

substrate: L-threonate


organism: Escherichia coli (strain K12)

substrate_name: L-galactonate

column_label: Abstract reports the Km and kcat for L-galactonate were 19.5+/-0.6 mM and 0.51+/-0.03 s(-1), respectively.

raw_value_unit_evidence: Km raw_value=19.5+/-0.6 mM raw_unit=mM

row_label: E. coli YjjN / L-galactonate

table_label: PubMed XML abstract PMID 24861318

substrate: L-galactonate


substrate_name: NAD+

substrate: NAD+


substrate_name: NADP+

substrate: NADP+


column_label: Table 1; row Q0K4F5 (RePdxA2) / d-Threonate 4-phosphate; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 3.4, 0.12, 2.9 x 10^4; normalized kcat/Km 29 s^-1 mM^-1

normalized_value_unit_evidence: kcat=3.4 s^-1; Km=0.12 mM; kcat/Km=29 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: Q0K4F5 (RePdxA2) / d-Threonate 4-phosphate: kcat=3.4 s^-1; KM=0.12 mM; kcat/KM=2.9 x 10^4 M^-1 s^-1

table_label: Table 1. Selected kinetic parameters for DtnK, PdxA2, LtnD, and DenD


column_label: Table 1; row Q0K4F5 (RePdxA2) / 4-Hydroxy-l-threonine 4-phosphate; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 0.35, 0.20, 1.8 x 10^3; normalized kcat/Km 1.8 s^-1 mM^-1

normalized_value_unit_evidence: kcat=0.35 s^-1; Km=0.2 mM; kcat/Km=1.8 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: Q0K4F5 (RePdxA2) / 4-Hydroxy-l-threonine 4-phosphate: kcat=0.35 s^-1; KM=0.2 mM; kcat/KM=1.8 x 10^3 M^-1 s^-1


row_label: Q0K4F5 (RePdxA2) / d-Threonate 4-phosphate


organism: Stenotrophomonas maltophilia

substrate_name: (2R/2S)-2-hexyl-3-oxodecanoic acid

smiles: CCCCCCCC(=O)C(CCCCCC)C(=O)O

proof_lines: Abstract supports the OleD substrate series and stereochemistry study.

proof_lines: No preserved row-level kinetic excerpt for (2R/2S)-2-hexyl-3-oxodecanoic acid.

substrate: (2R/2S)-2-hexyl-3-oxodecanoic acid


substrate_name: syn-2-decyl-3-hydroxytetradecanoic acid

proof_lines: Abstract identifies syn-2-decyl-3-hydroxytetradecanoic acid as the top substrate.

proof_lines: Saved evidence preserves relative catalytic efficiency, not the exact row constant.

substrate: syn-2-decyl-3-hydroxytetradecanoic acid


substrate_name: syn-2-octyl-3-hydroxydodecanoic acid

proof_lines: Abstract compares the octyl substrate with the decyl and hexyl analogs.

proof_lines: Saved evidence preserves only relative catalytic efficiency for the comparison set.

substrate: syn-2-octyl-3-hydroxydodecanoic acid


organism: Agrobacterium tumefaciens


substrate_name: D-xylonate

substrate: D-xylonate


substrate_name: L-Idonate

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

substrate: L-Idonate


substrate_name: D-gluconate

substrate: D-gluconate


substrate_name: D-Xylonate

proof_lines:
ThrDH homolog family
substrate-set context
D-Xylonate

substrate: D-Xylonate


substrate_name: D-Gluconate

proof_lines:
ThrDH homolog family
substrate-set context
D-Gluconate

substrate: D-Gluconate


substrate_name: 4-hydroxy-L-threonine 4-phosphate

column_label: Table 1; row P58718 (SePdxA2) / 4-Hydroxy-l-threonine 4-phosphate; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 0.37, 0.19, 1.9 x 10^3; normalized kcat/Km 1.9 s^-1 mM^-1

normalized_value_unit_evidence: kcat=0.37 s^-1; Km=0.19 mM; kcat/Km=1.9 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: P58718 (SePdxA2) / 4-Hydroxy-l-threonine 4-phosphate: kcat=0.37 s^-1; KM=0.19 mM; kcat/KM=1.9 x 10^3 M^-1 s^-1

substrate: 4-hydroxy-L-threonine 4-phosphate


column_label: Table 1; row P58718 (SePdxA2) / d-Threonate 4-phosphate; columns kcat (s^-1), KM (mM), kcat/KM (M^-1 s^-1); cells 8.9, 0.054, 1.6 x 10^5; normalized kcat/Km 160 s^-1 mM^-1

normalized_value_unit_evidence: kcat=8.9 s^-1; Km=0.054 mM; kcat/Km=160 s^-1 mM^-1 (explicit table value converted from M^-1 s^-1)

raw_value_unit_evidence: P58718 (SePdxA2) / d-Threonate 4-phosphate: kcat=8.9 s^-1; KM=0.054 mM; kcat/KM=1.6 x 10^5 M^-1 s^-1


substrate_name: D-tagaturonate

assay_conditions_summary: pH 7; 303.15 K; buffer pH 7; cofactor NADH

column_label: Table 1 row Bvu0222; D-tagaturonate row; kcat / KM / kcat/KM columns; footnote d reduction direction.

normalized_value_unit_evidence: 550 uM normalizes to 0.55 mM; 1.6 x 10^5 M^-1 s^-1 normalizes to 160 s^-1 mM^-1.

row_label: Bvu0222 / D-tagaturonate

table_label: Table 1: Catalytic Constants for Bvu0220, Bvu0219, and Bvu0222

substrate: D-tagaturonate


assay_conditions_summary: pH 7.5; 303.15 K; buffer pH 7; cofactor NAD+

column_label: Table 1 row Bvu0222; L-galactonate row; kcat / KM / kcat/KM columns.

normalized_value_unit_evidence: 36 uM normalizes to 0.036 mM; 1.7 x 10^4 M^-1 s^-1 normalizes to 17 s^-1 mM^-1.

row_label: Bvu0222 / L-galactonate


substrate_name: L-gluconate

column_label: Table 1 row Bvu0222; L-gluconate row; kcat / KM / kcat/KM columns.

normalized_value_unit_evidence: 510 uM normalizes to 0.51 mM; 3.9 x 10^2 M^-1 s^-1 normalizes to 0.39 s^-1 mM^-1.

row_label: Bvu0222 / L-gluconate

substrate: L-gluconate


enzyme_display_name: Retinol dehydrogenase 16

assay_conditions_summary: pH 7.3; cofactor NAD+

column_label: Table I row Androsterone, column Km (microM), reports 0.14 +/- 0.02.

raw_value_unit_evidence: Androsterone Km 0.14 +/- 0.02 microM

row_label: Androsterone

table_label: Table I. Kinetic constants of RoDH-4 for steroid substrates, PMID 9677409

enzyme: Retinol dehydrogenase 16


organism: Mus musculus

column_label: Table II row Androsterone has Activity 3alpha-HSD, Product androstanedione, Km 0.1 uM, Rate 6, V/Km 60.

normalized_value_unit_evidence: 0.1 uM = 0.0001 mM; CatLog row stores 0.0002 mM.

raw_value_unit_evidence: Table II reports Androsterone Km = 0.1 uM.

row_label: Androsterone / 3alpha-HSD / androstanedione

table_label: JBC 272(52) Table II, steroid substrate kinetics for recombinant mouse CRAD


enzyme_display_name: Perakine reductase

organism: Rauvolfia serpentina

substrate_name: coniferyl aldehyde

enzyme: Perakine reductase

substrate: coniferyl aldehyde


enzyme_display_name: Benzil reductase ((S)-benzoin forming) NRE1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: benzil (with NADH as cosubstrate)

proof_lines: Nre1p benzil NADH

substrate: benzil (with NADH as cosubstrate)


enzyme_display_name: Eugenol synthase 1

organism: Ocimum basilicum

substrate_name: NADPH (at pH 6.5 and 28 degrees Celsius)

column_label: Full text reports for EGS1 the corresponding Km values were 5.1 mM for coniferyl acetate and 131 microM for NADPH.

raw_value_unit_evidence: Km raw_value=131 microM raw_unit=microM

row_label: Ocimum basilicum EGS1 / NADPH cofactor

table_label: PMC full text PMID 16782809 EGS1/IGS1 kinetic prose

enzyme: Eugenol synthase 1


enzyme_display_name: benzil reductase [(S)-benzoin forming]

organism: Ogataea glucozyma

substrate_name: benzil

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines:
KRED1-Pglu
Pichia glucozyma
Ogataea glucozyma

enzyme: benzil reductase [(S)-benzoin forming]

substrate: benzil


organism: Sungouiella intermedia

substrate_name: xylitol

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

assay_conditions_summary: pH 7; cofactor NADP+

proof_lines:
cosubstrate NADP+, pH 7, 25°C
cosubstrate NAD+, pH 7, 25°C

substrate: xylitol


organism: Chlorobaculum tepidum

substrate_name: sepiapterin

proof_lines: For the reverse reaction, accepts L-threo-dihydrobiopterin, D-threo-dihydrobiopterin, L-threo-dihydroneopterin, dihydrotepidopterin and L-erythro-dihydrobiopterin as substrates.

substrate: sepiapterin


substrate_name: NADPH

assay_conditions_summary: pH 8.8; cofactor NADPH

substrate: NADPH


organism: Methanococcus maripaludis

substrate_name: NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

substrate: NAD+


organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

substrate_name: NAD (with CHMS as substrate at 25 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Official PMC Table 3 row NAD+ (200) lists CHMS Km=20.6 +/- 1.0 microM; the table footnote states that Km values are for the compounds shown in parentheses.

raw_value_unit_evidence: Km raw_value=20.6 +/- 1.0 microM raw_unit=microM for CHMS with NAD+

row_label: LigC / CHMS Km with NAD+ (200 microM cofactor)

table_label: PMC111406 Table 3, kinetic constants of the CHMS dehydrogenases


substrate_name: NADP (with CHMS as substrate at 25 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: Official PMC Table 3 row NADP+ (200) lists CHMS Km=26.0 +/- 0.5 microM; the table footnote states that Km values are for the compounds shown in parentheses.

raw_value_unit_evidence: Km raw_value=26.0 +/- 0.5 microM raw_unit=microM for CHMS with NADP+

row_label: LigC / CHMS Km with NADP+ (200 microM cofactor)