assay_conditions_summary: pH 8.5; cofactor CoA

column_label: Results prose lines 260-266 and Fig. 4; protein LBP; substrate C16:1DC-CoA ((2E)-hexadecenedioyl-CoA); metric apparent Km; raw value 0.3 uM; normalized Km=0.0003 mM.

raw_value_unit_evidence: Results text reports LBP apparent Km 0.3 uM for C16:1DC-CoA (Fig. 4).

table_label: PMID 15060085, Results prose and Fig. 4: kinetic analysis of human DBP and LBP


enzyme_display_name: Delta(3)-Delta(2)-enoyl-CoA isomerase

organism: Homo sapiens

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Results prose lines 260-266 and Fig. 4; protein LBP; substrate C16:1-CoA ((2E)-hexadecenoyl-CoA); metric apparent Km; raw value 10.4 uM; normalized Km=0.0104 mM.

raw_value_unit_evidence: Results text reports LBP apparent Km 10.4 uM for C16:1-CoA (Fig. 4).

data_origin: experimental

enzyme: Delta(3)-Delta(2)-enoyl-CoA isomerase

status: verified

source: uniprot


enzyme_display_name: pancreatic ribonuclease

substrate_name: poly(A)-poly(U)

source_db: brenda

verification_status: unverified

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

enzyme: pancreatic ribonuclease

substrate: poly(A)-poly(U)

status: unverified

source: brenda


mutation_type: substitution


proof_lines:
pH 7.5, 37°C, mutant G38D
G38D mutant


organism: Bos taurus

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


enzyme_display_name: methylitaconate Delta-isomerase

organism: Eubacterium barkeri

substrate_name: dimethylmaleate

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

column_label: Summary prose reports K_m value 4.0 x 10^-3 M for dimethylmaleate. Table IX lists MeIT isomerase substrate dimethylmaleate with Km 4.0 x 10^-3 M.

raw_value_unit_evidence: Km raw_value=4.0 x 10^-3 M raw_unit=M

row_label: MeIT isomerase / dimethylmaleate

table_label: JBC Summary prose and Table IX apparent Km and Vmax values

enzyme: methylitaconate Delta-isomerase

substrate: dimethylmaleate


enzyme_display_name: polyenoic fatty acid isomerase

organism: Cutibacterium acnes

substrate_name: linoleic acid

smiles: CCCCCC=CCC=CCCCCCCCC(=O)O

enzyme: polyenoic fatty acid isomerase

substrate: linoleic acid


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


organism: Rattus norvegicus

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8, hydratase activity, mutant enzyme K242D


proof_lines: pH 8, hydratase activity, mutant enzyme K242T


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


proof_lines: pH 8, hydratase activity, mutant enzyme K242C


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Bacillus sp. (in: firmicutes)

substrate_name: S-Benzyl-L-cysteine

enzyme: cysteine-S-conjugate beta-lyase

substrate: S-Benzyl-L-cysteine


substrate_name: L-selenodjenkolate

substrate: L-selenodjenkolate


substrate_name: L-djenkolate

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

substrate: L-djenkolate


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: S-methyl-L-cysteine

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

substrate: S-methyl-L-cysteine


organism: Ptilota filicina

sequence_source: multiple

smiles: CCC=CCC=CCC=CCC=CCC=CCCCC(=O)O

proof_lines: pH 7.2, assuming one catalytic site per enzyme molecule

source_databases_merged: brenda uniprot


proof_lines:
pH 7, 22°C
pH 9, 22°C


substrate_name: poly(A)poly(U)

substrate: poly(A)poly(U)


proof_lines:
wild-type, pH 7.5, 37°C
wild-type, 25°C, pH 5.0
pH 7.5, 37°C, wild-type enzyme


enzyme_display_name: leukotriene-C4 synthase

substrate_name: leukotriene A4

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R104S to reconstruct the assayed variant sequence.

proof_lines: mutant R104S, 22°C, pH not specified in the publication

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R104A to reconstruct the assayed variant sequence.

proof_lines: mutant R104A, 22°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31A to reconstruct the assayed variant sequence.

proof_lines: mutant R31A, 22°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R31Q to reconstruct the assayed variant sequence.

proof_lines: mutant R31Q, 22°C, pH not specified in the publication


proof_lines: wild-type, 22°C, pH not specified in the publication

proof_lines: pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme


enzyme_display_name: S-ribosylhomocysteine lyase

organism: Streptococcus suis

substrate_name: S-ribosylhomocysteine

enzyme: S-ribosylhomocysteine lyase

substrate: S-ribosylhomocysteine


assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

proof_lines:
pH 8.0, 25°C, MFE1
pH 8.0, 25°C, MECI
pH 8.0, 25°C, ECI


proof_lines:
pH 8.0, 25°C, MFE1
pH 8.0, 25°C, ECI
pH 8.0, 25°C, MECI


proof_lines:
pH 8.0, 25°C, MECI
pH 8.0, 25°C, MFE1
pH 8.0, 25°C, ECI


enzyme_display_name: protein disulfide-isomerase

organism: Mycothermus thermophilus

substrate_name: scrambled ribonuclease

enzyme: protein disulfide-isomerase

substrate: scrambled ribonuclease


organism: Bacillus subtilis

source_db: skid

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

proof_lines: kcat is 1471 min(-1) for isomerase activity with en-H2HPP as substrate.

source_databases_merged: skid uniprot

source: skid


enzyme_display_name: prostaglandin-D synthase

organism: Nilaparvata lugens

substrate_name: GSH

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

assay_conditions_summary: pH 8

proof_lines: at pH 8.0, temperature not specified in the publication

enzyme: prostaglandin-D synthase

substrate: GSH


organism: Corynebacterium glutamicum

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature C21S with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


proof_lines: recombinant wild-type enzyme, pH 7.6, 30°C


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature C24S with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


substrate_name: n Amyloid-beta protein 40; L-PGDS

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

substrate: n Amyloid-beta protein 40; L-PGDS


enzyme_display_name: D-tagatose 3-epimerase

organism: Cereibacter sphaeroides

substrate_name: D-fructose

source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R118W with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

enzyme: D-tagatose 3-epimerase

substrate: D-fructose

source: oed


column_label: Table 2; Table 2 WT row d-Fructose; WT enzyme columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 2 WT row d-Fructose reports Km 78 +/- 2.3 mM, kcat 42.60 +/- 0.89 s^-1, and kcat/Km 0.55 +/- 0.008 s^-1 mM^-1.

row_label: Table 2 WT row d-Fructose

table_label: PMID 29121933, Table 2: Kinetic parameters of RsDTE wild-type on four substrates


substrate_name: D-sorbose

substrate: D-sorbose


column_label: Table 2; Table 2 WT row d-Sorbose; WT enzyme columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

row_label: Table 2 WT row d-Sorbose


substrate_name: D-tagatose

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3IW04 and applied mutation signature R118W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 308.15 K; buffer 20 mM Tris–HCl

column_label: Table 2 (Kinetic parameters of RsDTE wild-type on four substrates), enzyme block 'R118W', substrate row 'd-Tagatose'; column 'Km (mM)' = 98 ± 3.5; column 'kcat (s-1)' = 51.25 ± 0.54; column 'kcat/Km (s-1 mM-1)' = 0.52 ± 0.013; column 'Relative activity (%)' = 100.

normalized_value_unit_evidence: Km: printed Table 2 cell 98 mM; mM is the canonical unit, so no unit conversion applies and the paper value is 98.0 mM. kcat: printed Table 2 cell 51.25 s^-1; s^-1 is the canonical unit, so no unit conversion applies and the paper value is 51.25 s^(-1). kcat/Km: printed Table 2 cell 0.52 s^-1 mM^-1; s^-1 mM^-1 is the canonical unit, so no unit conversion applies and the paper value is 0.52 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme block R118W, substrate row d-Tagatose: Km = 98 mM (printed as 98 ± 3.5); kcat = 51.25 s^-1 (printed as 51.25 ± 0.54); printed kcat/Km = 0.52 s^-1 mM^-1 (printed as 0.52 ± 0.013).

table_label: Table 2: Kinetic parameters of RsDTE wild-type on four substrates (Microb Cell Fact 2017, volume 16, article 193)

substrate: D-tagatose

status: corrected


column_label: Table 2; Table 2 WT row d-Tagatose; WT enzyme columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

row_label: Table 2 WT row d-Tagatose


substrate_name: D-Psicose

column_label: Table 2 (Kinetic parameters of RsDTE wild-type on four substrates), enzyme block 'R118W', substrate row 'd-Psicose'; column 'Km (mM)' = 193 ± 6.2; column 'kcat (s-1)' = 26.04 ± 0.58; column 'kcat/Km (s-1 mM-1)' = 0.14 ± 0.008; column 'Relative activity (%)' = 22.78.

normalized_value_unit_evidence: Km: printed Table 2 cell 193 mM; mM is the canonical unit, so no unit conversion applies and the paper value is 193.0 mM. kcat: printed Table 2 cell 26.04 s^-1; s^-1 is the canonical unit, so no unit conversion applies and the paper value is 26.04 s^(-1). kcat/Km: printed Table 2 cell 0.14 s^-1 mM^-1; s^-1 mM^-1 is the canonical unit, so no unit conversion applies and the paper value is 0.14 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme block R118W, substrate row d-Psicose: Km = 193 mM (printed as 193 ± 6.2); kcat = 26.04 s^-1 (printed as 26.04 ± 0.58); printed kcat/Km = 0.14 s^-1 mM^-1 (printed as 0.14 ± 0.008).

substrate: D-Psicose


column_label: Table 2; Table 2 WT row d-Psicose; WT enzyme columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

row_label: Table 2 WT row d-Psicose


enzyme_display_name: prostaglandin-E synthase

substrate_name: Prostaglandin H2

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

proof_lines: kcat is 50 sec(-1) for prostaglandin H2 as substrate (PubMed:12672824). kcat is 75 sec(-1) for prostaglandin H2 as substrate (PubMed:12672824). kcat is 21 sec(-1) for glutathione as substrate (PubMed:12672824).

source_databases_merged: sabio_rk skid uniprot

enzyme: prostaglandin-E synthase

substrate: Prostaglandin H2


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

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines:
at pH 8.0 and 37°C
at pH 8.0 and 25°C


substrate_name: prostaglandin H2

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y149A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y149A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C

substrate: prostaglandin H2


enzyme_display_name: lutein isomerase

organism: Danio rerio

substrate_name: all-trans-retinyl ester

proof_lines: kcat is 0.00044 sec(-1) with all-trans-retinyl ester as substrate.

enzyme: lutein isomerase

substrate: all-trans-retinyl ester


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q36E to reconstruct the assayed variant sequence.


organism: Gallus gallus

substrate_name: Unknown

substrate: Unknown


organism: Mus musculus

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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D176A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E196D to reconstruct the assayed variant sequence.


substrate_name: glutathione

substrate: glutathione


substrate_name: all-trans-retinyl palmitate

substrate: all-trans-retinyl palmitate


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature F83A to reconstruct the assayed variant sequence.

column_label: Table 2 row F83A, columns Km (uM) and Kcat (s^-1), cells 24.5 and 0.87; Figure 4 includes human L-PGDS sequence context.

raw_value_unit_evidence: Km 24.5 uM; Kcat 0.87 s^-1; Kcat/Km column 2.12 on the paper's minute/uM-like scale.

table_label: Table 2. Kinetic comparison between wild-type and mutant forms of human L-PGDS


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K59A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature L131A to reconstruct the assayed variant sequence.

column_label: Table 2 row L131A, columns Km (uM) and Kcat (s^-1), cells 25.2 and 0.81.

raw_value_unit_evidence: Km 25.2 uM; Kcat 0.81 s^-1; Kcat/Km column 1.89 on the paper's minute/uM-like scale.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature L79A to reconstruct the assayed variant sequence.

column_label: Table 2 row L79A, columns Km (uM) and Kcat (s^-1), cells 32.8 and 0.06.

raw_value_unit_evidence: Km 32.8 uM; Kcat 0.06 s^-1; Kcat/Km column 0.11 on the paper's minute/uM-like scale.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature M64A to reconstruct the assayed variant sequence.

column_label: Table 2 row M64A, columns Km (uM) and Kcat (s^-1), cells 32.5 and 0.63.

raw_value_unit_evidence: Km 32.5 uM; Kcat 0.63 s^-1; Kcat/Km column 1.17 on the paper's minute/uM-like scale.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature M94A to reconstruct the assayed variant sequence.

column_label: Table 2 row printed M94; prose identifies M94A mutation; columns Km (uM) and Kcat (s^-1), cells 20.2 and 2.24.

raw_value_unit_evidence: Km 20.2 uM; Kcat 2.24 s^-1; Kcat/Km column 6.66 on the paper's minute/uM-like scale.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature S45A to reconstruct the assayed variant sequence.

column_label: Table 2 row S45A, columns Km (uM) and Kcat (s^-1), cells 20.4 and 2.23.

raw_value_unit_evidence: Km 20.4 uM; Kcat 2.23 s^-1; Kcat/Km column 6.57 on the paper's minute/uM-like scale.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature S81A to reconstruct the assayed variant sequence.

column_label: Table 2 row S81A, columns Km (uM), Vmax, and Kcat, cells 18.5, 10.2, and 2.91.

raw_value_unit_evidence: Km 18.5 uM; Vmax 10.2 umol min^-1 mg^-1; Kcat 2.91 s^-1; Kcat/Km column 9.42.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature T147A to reconstruct the assayed variant sequence.

column_label: Table 2 row T147A, columns Km (uM) and Kcat (s^-1), cells 15.4 and 3.67.

raw_value_unit_evidence: Km 15.4 uM; Kcat 3.67 s^-1; Kcat/Km column 14.29 on the paper's minute/uM-like scale.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature W54A to reconstruct the assayed variant sequence.

column_label: Table 2 row W54A, columns Km (uM) and Kcat (s^-1), cells 16.1 and 2.40.

raw_value_unit_evidence: Km 16.1 uM; Kcat 2.40 s^-1; Kcat/Km column 8.94 on the paper's minute/uM-like scale.


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


column_label: Table 2 row Wild type, columns Km (uM) and Kcat (s^-1), cells 13.8 and 2.64.

raw_value_unit_evidence: Km 13.8 uM; Kcat 2.64 s^-1; Kcat/Km column 11.49 on the paper's minute/uM-like scale.

row_label: Wild type


sequence_variant_note: Resolved canonical sequence from uniprotkb:P41222;refseq:NP_000945.3 and applied mutation signature Y149A to reconstruct the assayed variant sequence.

column_label: Table 2 row Y149A, columns Km (uM) and Kcat (s^-1), cells 12.7 and 5.73; Figure 4 includes human L-PGDS sequence context.

raw_value_unit_evidence: Km 12.7 uM; Kcat 5.73 s^-1; Kcat/Km column 27.05 on the paper's minute/uM-like scale.


smiles: CCCCCC=CCC=CCC=CCC=CCCCCCC(=O)[O-]

assay_conditions_summary: pH 7; buffer A

column_label: Table 1 columns substrate adrenate (2) and Km (uM), row Km.

raw_value_unit_evidence: Table 1 adrenate (2) Km row: 17.0 +/- 1.5 uM.

row_label: adrenate (2)

table_label: Table 1: Kinetic Parameters of PFI with Various Substrates (+/-SE)


smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]

column_label: Table 1 columns substrate arachidonate (4) and Km (uM), row Km.

raw_value_unit_evidence: Table 1 arachidonate (4) Km row: 25.5 +/- 3.9 uM.

row_label: arachidonate (4)


smiles: CCCCCCCCC=CCC=CCC=CCCCC(=O)O

column_label: Table 1 columns substrate eicosatrienoate (7) and Km (uM), row Km.

raw_value_unit_evidence: Table 1 eicosatrienoate (7) Km row: 52.8 +/- 9.2 uM.

row_label: eicosatrienoate (7)


smiles: CCCCCC=CCC=CCC=CCCCCC(=O)O

column_label: Discussion text states gamma-linolenic acid (9) [(6Z,9Z,12Z)-octadecatrienoic acid] and gives Km=150 +/- 35 uM; the same discussion also mentions a 152 uM value from the earlier experiment.

raw_value_unit_evidence: Discussion prose for gamma-linolenic acid (9): Km=150 +/- 35 uM.

table_label: Discussion: Kinetic Parameters of Alternative Substrates


smiles: CCCCCCCCCC=CC=CC=CC=CC=CC=CC(=O)O

column_label: Table 1 columns substrate docosahexaenoate (1) and Km (uM), row Km.

raw_value_unit_evidence: Table 1 docosahexaenoate (1) Km row: 1.9 +/- 0.36 uM.

row_label: docosahexaenoate (1)


substrate_name: (7Z,10Z,13Z,16Z)-docosatetraenoic acid

smiles: CCCCCCCCCCCCCC=CC=CC=CC=CC(=O)O

substrate: (7Z,10Z,13Z,16Z)-docosatetraenoic acid


substrate_name: (5Z,8Z,11Z,14Z)-eicosatetraenoic acid

smiles: CCCCCCCCCCCC=CC=CC=CC=CC(=O)O

substrate: (5Z,8Z,11Z,14Z)-eicosatetraenoic acid


column_label: Figure 6C caption says liposomes with increasing concentrations of all-trans retinyl palmitate were incubated with purified RPE65; Results prose reports Km was 3.7 uM.

normalized_value_unit_evidence: Km central normalized_value=0.0037 normalized_unit=mM.

raw_value_unit_evidence: Results prose reports Michaelis constant Km raw_value=3.7 raw_unit=uM for purified RPE65.

row_label: Purified recombinant chicken RPE65

table_label: PMC2777724 Figure 6C and Results prose


substrate_name: Prostaglandin G2

substrate: Prostaglandin G2


enzyme_display_name: UniProt Q16647

substrate_name: 15-hydroperoxyeicosatetraenoic acid

source_license: CC BY-NC-ND 4.0

smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)O)OO

enzyme: UniProt Q16647

substrate: 15-hydroperoxyeicosatetraenoic acid


substrate_name: 11-cis retinol

column_label: PMC full text states that Lineweaver-Burk analysis yielded, for 11cROL, Km = 1.91 uM and Vmax = 1.82 nmol/mg total protein/hr.

raw_value_unit_evidence: Km raw_value=1.91 uM raw_unit=uM

row_label: zebrafish RPE65c 11cROL product channel from atRE-liposome assay

table_label: PMC3354629 Results prose / Figure 5 kinetic parameters

substrate: 11-cis retinol


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


substrate_name: glutathione for the glutathione-conjugating activity


column_label: JBC Table I, row WT, column GST activity K m(CDNB), reports 3.00 mM.

raw_value_unit_evidence: Km raw_value=3.00 raw_unit=mM

row_label: WT

table_label: Table I. Kinetic parameters of wild-type and mutant PGDSs


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y117S with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R70A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T129V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R70A/R122A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y117A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


enzyme_display_name: styrene-oxide isomerase

organism: Corynebacterium sp.

substrate_name: styrene oxide

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

enzyme: styrene-oxide isomerase

substrate: styrene oxide


organism: Homo sapiens


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


enzyme_display_name: prostaglandin-I synthase

enzyme: prostaglandin-I synthase


substrate_name: reduced PGIS; Carbon monoxide

substrate: reduced PGIS; Carbon monoxide


enzyme_display_name: thromboxane-A synthase

organism: Sus scrofa

enzyme: thromboxane-A synthase


enzyme_display_name: allene-oxide cyclase

organism: Solanum lycopersicum

proof_lines: kcat is 820 sec(-1) with 9-HPOD as substrate. kcat is 236 sec(-1) with 9-HPOT as substrate. kcat is 99 sec(-1) with 13-HPOD as substrate. kcat is 21 sec(-1) with 13-HPOT as substrate.

enzyme: allene-oxide cyclase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S45A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W54A/H111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S45A/T67A/S81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W45A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S81A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P110A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S45A/T67A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T67A/S81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T67A to reconstruct the assayed variant sequence.


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


substrate: glutathione for the glutathione-conjugating activity


organism: Bos taurus


organism: Rattus norvegicus

substrate_name: reduced glutathione

substrate: reduced glutathione


column_label: Table 3 row PGDS activity / Km for PGH2 (mM) reports 0.2 for both hPGDS and rPGDS; the text states hPGDS, rPGDS, and mPGDS enzymes have obtained similar 200 uM PGH2 Km values.

raw_value_unit_evidence: Km raw_value=0.2 mM raw_unit=mM

row_label: PGDS activity / Km for PGH2

table_label: Table 3, PMID 10824118 PDF


substrate_name: Prostaglandin H1

column_label: Results prose reports: using PGH1 as substrate, PGIS exhibited Km = 6.2 +/- 1.2 uM and Vmax = 2400 +/- 200 mole MDA/min/mole, equivalent to 40 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.0062 normalized_unit=mM; Vmax normalized_value=40 normalized_unit=s^-1 equivalent

raw_value_unit_evidence: Km raw_value=6.2 +/- 1.2 uM; Vmax raw_value=2400 +/- 200 mole MDA/min/mole

row_label: PGH1 steady-state kinetic prose

table_label: PMC PMID 16406803 Results prose

substrate: Prostaglandin H1


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


substrate_name: prostaglandin H2 (at 23 degrees Celsius)


enzyme_display_name: capsanthin/capsorubin synthase

organism: Capsicum annuum

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: capsanthin/capsorubin synthase

substrate: NADPH


organism: Saccharina japonica

substrate_name: alpha-D-glucose 1-phosphate

proof_lines:
at pH 7.0 and 30°C
at pH 7.5 and 30°C

substrate: alpha-D-glucose 1-phosphate


substrate_name: prostaglandin H2

column_label: Official PubMed XML abstract reports PGH2 Km = 130 microM, not the exported 0.037 mM PGH2 value.

normalized_value_unit_evidence: Km normalized_value=0.13 normalized_unit=mM for PGH2

raw_value_unit_evidence: Km raw_value=130 raw_unit=microM for PGH2

row_label: Recombinant mouse microsomal prostaglandin E synthase-1 membrane fraction

table_label: Official PubMed XML abstract kinetic prose

substrate: prostaglandin H2


column_label: Official PubMed XML abstract reports GSH Km = 37 microM, not the exported 0.13 mM glutathione value.

normalized_value_unit_evidence: Km normalized_value=0.037 normalized_unit=mM for GSH

raw_value_unit_evidence: Km raw_value=37 raw_unit=microM for GSH


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


substrate_name: PGH2 (for the GSH-heme complex-bound enzyme)

column_label: Abstract reports KM = 56 microM for PGH2 degradation by mPGES-2h.

raw_value_unit_evidence: Km raw_value=56 microM raw_unit=microM

row_label: mPGES-2h / PGH2 degradation

table_label: PubMed XML abstract PMID 17585783


substrate_name: Prostaglandin H2

substrate: Prostaglandin H2


organism: Macaca fascicularis


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)[O-])OO


organism: Giardia duodenalis

proof_lines: PGM2, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C

proof_lines: PGM1, in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C


organism: Pyrococcus horikoshii

proof_lines:
isoenzyme PH0923, 37°C
isoenzyme PH0923, 65°C
isoenzyme PH0923S101A, 65°C


organism: Lactococcus lactis


substrate_name: Unknown

substrate: Unknown


organism: Senna corymbosa


organism: Xanthomonas citri pv. citri


organism: Saccharomyces cerevisiae

substrate_name: D-Glucose 1-phosphate

substrate: D-Glucose 1-phosphate


organism: Toxoplasma gondii

proof_lines: isozyme PGM-II, in 50 mM HEPES-KOH, pH 8.0, at 37°C

proof_lines: isozyme PGM-I, in 50 mM HEPES-KOH, pH 8.0, at 37°C


organism: Saccharolobus solfataricus

substrate_name: D-glucose 6-phosphate

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

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

substrate: D-glucose 6-phosphate


enzyme_display_name: D-galactarolactone isomerase

organism: Agrobacterium tumefaciens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N240D with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N240D, pH and temperature not specified in the publication

enzyme: D-galactarolactone isomerase


organism: Pseudomonas aeruginosa

proof_lines: kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1) for mannose 1-phosphate.


organism: Agrobacterium fabrum (strain C58 / ATCC 33970)


organism: Sphingomonas sanxanigenens

proof_lines: recombinant His-tagged enzyme, pH 7.6, temperature not specified in the publication


organism: Homo sapiens

substrate_name: alpha-D-Glucose 1-phosphate

source_databases_merged: sabio_rk brenda uniprot

substrate: alpha-D-Glucose 1-phosphate


enzyme_display_name: 2-methylfumaryl-CoA isomerase

organism: Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 840 sec(-1) for isomerase activity with 2-methylfumaryl-CoA.

enzyme: 2-methylfumaryl-CoA isomerase


organism: Arabidopsis thaliana


organism: Drosophila melanogaster


organism: Plasmodium falciparum (isolate 3D7)

sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

proof_lines: kcat is 0.00017 sec(-1) for the conversion of mannose 6-phosphate (M6P) to mannose 1-phosphate (M1P) in the presence of glucose-1,6-bisphosphate (G-1,6-P) (at room temperature). kcat is 0.0000078 sec(-1) for the conversion of glucose 1-phos


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


proof_lines: recombinant His-tagged Pgm1, pH 7.5, 30°C


organism: Thermococcus kodakarensis

proof_lines: kcat is 575 sec(-1) with glucose 1-phosphate as substrate. kcat is 330 sec(-1) with mannose 1-phosphate as substrate. kcat is 190 sec(-1) with 2-deoxyribose 1-phosphate as substrate.


substrate_name: mannose 6-phosphate (M6P) (at room temperature)


substrate_name: glucose 1-phosphate (G1P) (at room temperature)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature D263G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row D263G; column 'kcat' with printed unit s^-1 = 3.0; column 'Km' with printed unit uM = 115; column 'kcat/Km' with printed unit uM^-1 s^-1 = 0.026.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.0 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 3.0 s^(-1). Km: printed Table 2 cell 115 in the column unit uM; 1 uM is 0.001 mM, so 115 / 1000 = 0.115 mM. kcat/Km: printed Table 2 cell 0.026 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.026 x 1000 = 26.0 s^(-1)*mM^(-1), while the catalog carries 26.08695652173913 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row D263G: kcat = 3.0 s^-1; Km = 115 uM; printed kcat/Km = 0.026 uM^-1 s^-1.

row_label: Table 2, body row D263G

table_label: Table 2: Kinetic parameters and phosphorylation state of WT PGM1 and missense variants (J. Biol. Chem. 2014, 289(46):32010-32019)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature D263Y to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row D263Y; column 'kcat' with printed unit s^-1 = 1.54; column 'Km' with printed unit uM = 170; column 'kcat/Km' with printed unit uM^-1 s^-1 = 0.0091.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.54 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 1.54 s^(-1). Km: printed Table 2 cell 170 in the column unit uM; 1 uM is 0.001 mM, so 170 / 1000 = 0.17 mM. kcat/Km: printed Table 2 cell 0.0091 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.0091 x 1000 = 9.1 s^(-1)*mM^(-1), while the catalog carries 9.058823529411764 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row D263Y: kcat = 1.54 s^-1; Km = 170 uM; printed kcat/Km = 0.0091 uM^-1 s^-1.

row_label: Table 2, body row D263Y


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature D62H to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row D62H; column 'kcat' with printed unit s^-1 = 0.197; column 'Km' with printed unit uM = 23.3; column 'kcat/Km' with printed unit uM^-1 s^-1 = 0.0085.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.197 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 0.197 s^(-1). Km: printed Table 2 cell 23.3 in the column unit uM; 1 uM is 0.001 mM, so 23.3 / 1000 = 0.0233 mM. kcat/Km: printed Table 2 cell 0.0085 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.0085 x 1000 = 8.5 s^(-1)*mM^(-1), while the catalog carries 8.565217391304348 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row D62H: kcat = 0.197 s^-1; Km = 23.3 uM; printed kcat/Km = 0.0085 uM^-1 s^-1.

row_label: Table 2, body row D62H


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature G121R to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row G121R; column 'kcat' with printed unit s^-1 = 0.368; column 'Km' with printed unit uM = 56; column 'kcat/Km' with printed unit uM^-1 s^-1 = 0.0066.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.368 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 0.368 s^(-1). Km: printed Table 2 cell 56 in the column unit uM; 1 uM is 0.001 mM, so 56 / 1000 = 0.056 mM. kcat/Km: printed Table 2 cell 0.0066 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.0066 x 1000 = 6.6 s^(-1)*mM^(-1), while the catalog carries 6.571428571428571 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row G121R: kcat = 0.368 s^-1; Km = 56 uM; printed kcat/Km = 0.0066 uM^-1 s^-1.

row_label: Table 2, body row G121R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature K68M to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row K68M; column 'kcat' with printed unit s^-1 = 153; column 'Km' with printed unit uM = 63.8; column 'kcat/Km' with printed unit uM^-1 s^-1 = 2.40.

normalized_value_unit_evidence: kcat: printed Table 2 cell 153 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 153.0 s^(-1). Km: printed Table 2 cell 63.8 in the column unit uM; 1 uM is 0.001 mM, so 63.8 / 1000 = 0.0638 mM. kcat/Km: printed Table 2 cell 2.40 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 2.40 x 1000 = 2400.0 s^(-1)*mM^(-1), while the catalog carries 2390.625 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row K68M: kcat = 153 s^-1; Km = 63.8 uM; printed kcat/Km = 2.40 uM^-1 s^-1.

row_label: Table 2, body row K68M


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature R221C to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row R221C; column 'kcat' with printed unit s^-1 = 200; column 'Km' with printed unit uM = 94; column 'kcat/Km' with printed unit uM^-1 s^-1 = 2.1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 200 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 200.0 s^(-1). Km: printed Table 2 cell 94 in the column unit uM; 1 uM is 0.001 mM, so 94 / 1000 = 0.094 mM. kcat/Km: printed Table 2 cell 2.1 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 2.1 x 1000 = 2100.0 s^(-1)*mM^(-1), while the catalog carries 2127.659574468085 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row R221C: kcat = 200 s^-1; Km = 94 uM; printed kcat/Km = 2.1 uM^-1 s^-1.

row_label: Table 2, body row R221C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature T115A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row T115A; column 'kcat' with printed unit s^-1 = 36.0; column 'Km' with printed unit uM = 41; column 'kcat/Km' with printed unit uM^-1 s^-1 = 0.88.

normalized_value_unit_evidence: kcat: printed Table 2 cell 36.0 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 36.0 s^(-1). Km: printed Table 2 cell 41 in the column unit uM; 1 uM is 0.001 mM, so 41 / 1000 = 0.041 mM. kcat/Km: printed Table 2 cell 0.88 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.88 x 1000 = 880.0 s^(-1)*mM^(-1), while the catalog carries 878.0487804878048 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row T115A: kcat = 36.0 s^-1; Km = 41 uM; printed kcat/Km = 0.88 uM^-1 s^-1.

row_label: Table 2, body row T115A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature T19A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row T19A; column 'kcat' with printed unit s^-1 = 0.685; column 'Km' with printed unit uM = 130; column 'kcat/Km' with printed unit uM^-1 s^-1 = 0.0053.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.685 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 0.685 s^(-1). Km: printed Table 2 cell 130 in the column unit uM; 1 uM is 0.001 mM, so 130 / 1000 = 0.13 mM. kcat/Km: printed Table 2 cell 0.0053 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.0053 x 1000 = 5.3 s^(-1)*mM^(-1), while the catalog carries 5.269230769230769 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row T19A: kcat = 0.685 s^-1; Km = 130 uM; printed kcat/Km = 0.0053 uM^-1 s^-1.

row_label: Table 2, body row T19A


column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row WT; column 'kcat' with printed unit s^-1 = 143; column 'Km' with printed unit uM = 80; column 'kcat/Km' with printed unit uM^-1 s^-1 = 1.8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 143 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 143.0 s^(-1). Km: printed Table 2 cell 80 in the column unit uM; 1 uM is 0.001 mM, so 80 / 1000 = 0.08 mM. kcat/Km: printed Table 2 cell 1.8 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.8 x 1000 = 1800.0 s^(-1)*mM^(-1), while the catalog carries 1787.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row WT: kcat = 143 s^-1; Km = 80 uM; printed kcat/Km = 1.8 uM^-1 s^-1.

row_label: Table 2, body row WT


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P36871 and applied mutation signature Y420H to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters and phosphorylation state of WT PGM1 and missense variants), body row Y420H; column 'kcat' with printed unit s^-1 = 162; column 'Km' with printed unit uM = 75; column 'kcat/Km' with printed unit uM^-1 s^-1 = 2.1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 162 in the column unit s^-1; the column prints reciprocal seconds, so no unit conversion applies and the value carries over as 162.0 s^(-1). Km: printed Table 2 cell 75 in the column unit uM; 1 uM is 0.001 mM, so 75 / 1000 = 0.075 mM. kcat/Km: printed Table 2 cell 2.1 in the column unit uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 2.1 x 1000 = 2100.0 s^(-1)*mM^(-1), while the catalog carries 2160.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, body row Y420H: kcat = 162 s^-1; Km = 75 uM; printed kcat/Km = 2.1 uM^-1 s^-1.

row_label: Table 2, body row Y420H


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: 2-deoxyribose 1-phosphate

substrate: 2-deoxyribose 1-phosphate


organism: Acetobacter xylinus

substrate_name: D-Glucose 1,6-bisphosphate

substrate: D-Glucose 1,6-bisphosphate


substrate_name: Glycerate 1,3-bisphosphate; D-Glucose 1-phosphate


substrate_name: H2O; alpha-D-Glucose 1,6-bisphosphate

substrate: H2O; alpha-D-Glucose 1,6-bisphosphate


substrate_name: alpha-D-Glucose 1,6-bisphosphate; H2O

substrate: alpha-D-Glucose 1,6-bisphosphate; H2O


enzyme_display_name: phosphoglucomutase

organism: Rattus norvegicus

enzyme: phosphoglucomutase


substrate_name: alpha-D-Glucose 6-phosphate

substrate: alpha-D-Glucose 6-phosphate


substrate_name: Glucose 1-phosphate

substrate: Glucose 1-phosphate


substrate_name: 2-deoxy-alpha-D-ribose 1-phosphate

substrate: 2-deoxy-alpha-D-ribose 1-phosphate


assay_conditions_summary: pH 6


organism: Saccharomyces cerevisiae


substrate_name: alpha-D-Ribose 1-phosphate

substrate: alpha-D-Ribose 1-phosphate


organism: Lactococcus lactis subsp. cremoris

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


organism: Escherichia coli (strain K12)


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

substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


substrate_name: mannose 6-phosphate

substrate: mannose 6-phosphate


organism: Chloroflexus aurantiacus

assay_conditions_summary: 328.15 K; cofactor CoA

proof_lines: 55°C, pH not specified in the publication


substrate_name: alpha-D-glucose 1,6-diphosphate

column_label: Abstract reports Km values for glucose 1-phosphate and glucose 1,6-bisphosphate were 2.34 times 10(-5) M and 2.24 times 10(-6) M, respectively.

raw_value_unit_evidence: Km raw_value=2.24 x 10(-6) M raw_unit=M

row_label: Fleischmann yeast phosphoglucomutase / glucose 1,6-bisphosphate

table_label: PubMed XML abstract PMID 1100398

substrate: alpha-D-glucose 1,6-diphosphate


organism: Pseudomonas aeruginosa

substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


proof_lines:
R247A mutant
mutant R247A


organism: Mycobacterium tuberculosis


organism: Triticum aestivum


organism: Bacillus subtilis


organism: Sus scrofa

substrate_name: prostaglandin H2

column_label: PubMed abstract states the enzyme reaction has a Km for 15-hydroxy-9 alpha, 11 alpha-peroxidoprosta-5, 13-dienoic acid of 12 microM, with optimal pH 7.5 and 30 degrees C.

raw_value_unit_evidence: Km raw_value=12 raw_unit=microM

row_label: porcine lung thromboxane synthase with 15-hydroxy-9 alpha,11 alpha-peroxidoprosta-5,13-dienoic acid (prostaglandin H2)

table_label: PubMed abstract PMID 3745158

substrate: prostaglandin H2


enzyme_display_name: ribonuclease T2

organism: Aspergillus oryzae

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

enzyme: ribonuclease T2


enzyme_display_name: Delta(3)-Delta(2)-enoyl-CoA isomerase

proof_lines:
pI 6.83 enzyme
pI 7.01 enzyme
pI 6.57 enzyme

enzyme: Delta(3)-Delta(2)-enoyl-CoA isomerase


proof_lines:
pI 6.83 enzyme
pI 7.01 enzyme


smiles: CCCCCCC#CCC(=O)N(CCS)C(=O)C

proof_lines:
pI 6.57 enzyme
pI 7.01 enzyme
pI 6.83 enzyme


smiles: CCCCCCCCCC#CC(=O)C(CNC(=O)C)S


smiles: CCCCCC#CC(=O)C(CNC(=O)C)S

proof_lines:
pI 7.01 enzyme
pI 6.57 enzyme
pI 6.83 enzyme


enzyme_display_name: protoporphyrin ferrochelatase

proof_lines: wild type enzyme, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication

enzyme: protoporphyrin ferrochelatase


proof_lines: mutant enzyme Y13M, in 100 mM tris(hydroxymethyl)aminomethane-HCl, pH 7.4, temperature not specified in the publication


proof_lines: wild-type, in the presence of 4 mM Mg2+, pH 7.4, room temperature


enzyme_display_name: pancreatic ribonuclease

organism: Bos taurus

substrate_name: cytidine-2',3'-cyclic monophosphate

enzyme: pancreatic ribonuclease

substrate: cytidine-2',3'-cyclic monophosphate


enzyme_display_name: prostaglandin-D synthase

organism: Homo sapiens

proof_lines: mutant enzyme L79A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C

enzyme: prostaglandin-D synthase


proof_lines: mutant enzyme M64A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: mutant enzyme L131A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: mutant enzyme F83A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: mutant enzyme S45A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: mutant enzyme M94A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: mutant enzyme W54A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: wild type enzyme, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: mutant enzyme S81A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: mutant enzyme T147A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


proof_lines: mutant enzyme K59A, in 100 mM Tris-HCl (pH 8.0), 100 mM NaCl, and 1 mM dithiothreitol, at 25°C


organism: Aspergillus phoenicis

substrate_name: ApA

substrate: ApA


substrate_name: ApG

substrate: ApG


organism: Caulobacter vibrioides


substrate_name: mesoporphyrin IX

substrate: mesoporphyrin IX


enzyme_display_name: methionine gamma-lyase

organism: Citrobacter freundii

substrate_name: L-methionine

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

enzyme: methionine gamma-lyase

substrate: L-methionine


substrate_name: mesoporphyrin

substrate: mesoporphyrin


substrate_name: protoporphyrin

substrate: protoporphyrin


enzyme_display_name: protein disulfide-isomerase

substrate_name: dithiothreitol

smiles: C(C(C(CS)O)O)S

proof_lines: with scrambled ribonuclease as substrate

enzyme: protein disulfide-isomerase

substrate: dithiothreitol


smiles: C(CS)O


substrate_name: cysteine

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

proof_lines: glutathione, with scrambled ribonuclease as substrate

substrate: cysteine


substrate_name: GSH

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

substrate: GSH


substrate_name: methiin

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

proof_lines: PEGylated mutant enzyme C115H, at pH 8.0 and 30°C

proof_lines: liposomes and polymeric vesicles-bound mutant enzyme C115H, at pH 8.0 and 30°C

substrate: methiin


substrate_name: alliin

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

substrate: alliin


substrate_name: propiin

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

proof_lines: free mutant enzyme C115H, at pH 8.0 and 30°C

substrate: propiin


substrate_name: S-methyl-L-cysteine

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

substrate: S-methyl-L-cysteine


proof_lines: mutant H388A, co-expressed with wild-type, 37°C

proof_lines: mutant C395delta, co-expressed with wild-type, 37°C


proof_lines: mutant H263A, co-expressed with wild-type, 37°C

proof_lines: mutant I186T, co-expressed with wild-type, 37°C


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Escherichia coli

substrate_name: L-cystathionine

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystathionine


proof_lines: pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sC-eCBL

proof_lines: pH 8.5, 25°C, recombinant chimeric mutant enzyme eCGS-sN-eCBL


enzyme_display_name: leukotriene-C4 synthase

substrate_name: glutathione

enzyme: leukotriene-C4 synthase

substrate: glutathione


substrate_name: leukotriene A4

substrate: leukotriene A4


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: D-ribose 1-phosphate

column_label: Table 3 row Pgm2 under ribose-1-phosphate has Vmax, km, and kcat/km columns; values are 0.32, 530, and 0.63 respectively

raw_value_unit_evidence: Ribose-1-phosphate columns report Vmax=0.32 +/- 0.01 umol/(min mgprot), km=530 +/- 3 uM, kcat/km=0.63

row_label: Pgm2 / ribose-1-phosphate

table_label: Table 3. Kinetic parameters of purified His-tagged Pgm proteins on glucose-1-phosphate and ribose-1-phosphate

substrate: D-ribose 1-phosphate


organism: Lacticaseibacillus casei

substrate_name: L-cysteine

proof_lines:
Ctl2, at pH 5.5 and 37°C
Ctl1, at pH 5.5 and 37°C

substrate: L-cysteine


assay_conditions_summary: pH 5.5; 310.15 K; buffer sodium phosphate

proof_lines: Ctl2, in sodium phosphate buffer, at pH 5.5 and 37°C

proof_lines: Ctl1, in sodium phosphate buffer, at pH 5.5 and 37°C

proof_lines: Ctl1, in sodium phosphate buffer, at pH 6.8 and 37°C


substrate_name: DL-homocysteine

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

substrate: DL-homocysteine


proof_lines:
Ctl1, at pH 5.5 and 37°C
Ctl2, at pH 5.5 and 37°C


organism: Myxococcus xanthus


substrate_name: mesoporphyrin IX

substrate: mesoporphyrin IX


organism: Trypanosoma brucei

proof_lines: 37°C, pH 8, 50 mM sodium phosphate, Q81N


proof_lines: 37°C, pH 8, 50 mM sodium phosphate, wild-type


organism: Mus musculus

substrate_name: protoporphyrin IX

proof_lines: wild-type, under strictly anaerobic conditions

substrate: protoporphyrin IX


proof_lines: mutant P255R, under strictly anaerobic conditions


enzyme_display_name: adenylate cyclase

organism: Bordetella pertussis

substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: mutant enzyme R338A/D360A, at pH 8.0 and 30°C

enzyme: adenylate cyclase

substrate: ATP


enzyme_display_name: UniProt P77366

substrate_name: beta-D-glucose 6-phosphate

enzyme: UniProt P77366

substrate: beta-D-glucose 6-phosphate


enzyme_display_name: UniProt Q818Z9

organism: Bacillus cereus

substrate_name: D-ribose 5-phosphate

enzyme: UniProt Q818Z9

substrate: D-ribose 5-phosphate


enzyme_display_name: phosphomannomutase

organism: Saccharina japonica

substrate_name: alpha-D-glucose 1-phosphate

enzyme: phosphomannomutase

substrate: alpha-D-glucose 1-phosphate


organism: Amorphophallus konjac

substrate_name: mannose 1-phosphate

substrate: mannose 1-phosphate


enzyme_display_name: UniProt P56839

organism: Mytilus edulis

enzyme: UniProt P56839


enzyme_display_name: L-3-cyanoalanine synthase

organism: Solanum tuberosum

substrate_name: CN-

enzyme: L-3-cyanoalanine synthase

substrate: CN-


substrate_name: O-acetyl-L-serine

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

substrate: O-acetyl-L-serine


organism: Porphyromonas gingivalis

substrate_name: S-ethyl-L-homocysteine

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

substrate: S-ethyl-L-homocysteine


substrate_name: L-methionine sulfoxide

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

substrate: L-methionine sulfoxide


substrate_name: S-Benzyl-L-cysteine

substrate: S-Benzyl-L-cysteine


substrate_name: S-ethyl-L-cysteine

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

substrate: S-ethyl-L-cysteine


organism: Cavia porcellus

substrate_name: leukotriene A4

substrate: leukotriene A4


substrate_name: 14,15-Leukotriene A4 methyl ester

substrate: 14,15-Leukotriene A4 methyl ester


substrate_name: 14,15-Leukotriene A4

substrate: 14,15-Leukotriene A4


organism: Bos taurus


substrate_name: cytidine-2',3'-cyclic monophosphate

substrate: cytidine-2',3'-cyclic monophosphate


enzyme_display_name: phosphopentomutase

organism: Rattus norvegicus

substrate_name: deoxyribose 1-phosphate

enzyme: phosphopentomutase

substrate: deoxyribose 1-phosphate


substrate_name: ribose 1-phosphate

substrate: ribose 1-phosphate


enzyme_display_name: beta-phosphoglucomutase

organism: Pyrococcus sp.

substrate_name: beta-D-glucose 1-phosphate

proof_lines:
Raw SKiD Env: Temp=90°C, pH=6
Raw SKiD Env: Temp=90°C, pH=-----

enzyme: beta-phosphoglucomutase

substrate: beta-D-glucose 1-phosphate


enzyme_display_name: phosphoglucomutase (glucose-cofactor)

organism: Escherichia coli

proof_lines: direct assay with unreacted glucose 1-phosphate

proof_lines: assay coupled with glucose-6-phosphate dehydrogenase, following NADPH formation

enzyme: phosphoglucomutase (glucose-cofactor)


substrate_name: alpha-D-glucose

substrate: alpha-D-glucose


enzyme_display_name: phosphoacetylglucosamine mutase

organism: Blastocladiella emersonii

substrate_name: N-acetylglucosamine 6-phosphate

enzyme: phosphoacetylglucosamine mutase

substrate: N-acetylglucosamine 6-phosphate


enzyme_display_name: protoporphyrin ferrochelatase

substrate_name: hematoporphyrin

enzyme: protoporphyrin ferrochelatase

substrate: hematoporphyrin


organism: Euglena gracilis

substrate_name: beta-D-Glucose 1-phosphate

substrate: beta-D-Glucose 1-phosphate


organism: Senna corymbosa

substrate_name: D-mannose 1-phosphate

substrate: D-mannose 1-phosphate


substrate_name: D-mannose 6-phosphate

substrate: D-mannose 6-phosphate


organism: Pyrococcus horikoshii

proof_lines:
isoenzyme PH0923, 37°C
isoenzyme PH0923, 65°C
isoenzyme PH0923S101A, 65°C


proof_lines: 90°C, pH not specified in the publication


organism: Giardia duodenalis


organism: Mus musculus

substrate_name: prostaglandin H2

mutation_signature: Δ1

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

mutation_type: deletion

substrate: prostaglandin H2


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature S45A/S81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature H116A to reconstruct the assayed variant sequence.


enzyme_display_name: pancreatic ribonuclease

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

enzyme: pancreatic ribonuclease


substrate_name: alpha-D-mannose 1-phosphate

proof_lines: in 50 mM HEPES, pH 7.1, 5 mM MgCl2, at 30°C

substrate: alpha-D-mannose 1-phosphate


enzyme_display_name: phosphoenolpyruvate mutase

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E114A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

enzyme: phosphoenolpyruvate mutase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D58N to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme D58N, at pH 7.5 and 25°C
mutant D58N, 25°C, pH 7.5


substrate_name: cyclic 2',3'-cytidine monophosphate

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +26, so it is treated as a source-provided variant sequence.

proof_lines:
mutant K7H/R10H, pH 5.5, 25°C
mutant K7H/R10H, pH 7.0

substrate: cyclic 2',3'-cytidine monophosphate


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

proof_lines:
wild-type, pH 5.5, 25°C
wild-type, pH 7.0
wild-type, pH7.0


substrate_name: pentacytidylic acid

assay_conditions_summary: pH 7

substrate: pentacytidylic acid


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

substrate_name: glucose 6-phosphate

proof_lines: kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1) for mannose 1-phosphate.

substrate: glucose 6-phosphate


substrate_name: mannose 6-phosphate

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

substrate: mannose 6-phosphate


organism: Arabidopsis thaliana

column_label: Figure 4 caption reports mannose-1-phosphate reaction Km 29.7 uM for recombinant AtPMM

raw_value_unit_evidence: Figure 4 Km raw_value=29.7 raw_unit=uM

row_label: Recombinant Arabidopsis phosphomannomutase AtPMM

table_label: Wiley full text Figure 4


column_label: Figure 4 caption reports glucose-1-phosphate reaction Km 65.4 uM for recombinant AtPMM

raw_value_unit_evidence: Figure 4 Km raw_value=65.4 raw_unit=uM


organism: Homo sapiens

substrate_name: alpha-D-Glucose 1-phosphate

proof_lines:
isoform alpha-PMM1, pH 6.5, 25°C
recombinant enzyme PMM1
isoform PMM1, at pH 7.5 and 32°C

source_databases_merged: sabio_rk brenda skid uniprot

substrate: alpha-D-Glucose 1-phosphate


organism: Thermococcus kodakarensis

proof_lines: kcat is 575 sec(-1) with glucose 1-phosphate as substrate. kcat is 330 sec(-1) with mannose 1-phosphate as substrate. kcat is 190 sec(-1) with 2-deoxyribose 1-phosphate as substrate.


enzyme_display_name: phosphoglucosamine mutase

organism: Escherichia coli (strain K12)

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

enzyme: phosphoglucosamine mutase


organism: Sus scrofa

substrate_name: galactose 1,6-diphosphate

substrate: galactose 1,6-diphosphate


enzyme_display_name: bisphosphoglycerate mutase

organism: Gallus gallus

substrate_name: H2O; 2,3-Bisphosphoglycerate

enzyme: bisphosphoglycerate mutase

substrate: H2O; 2,3-Bisphosphoglycerate


organism: Lactococcus lactis subsp. lactis

substrate_name: H2O; 4-Nitrophenyl phosphate

substrate: H2O; 4-Nitrophenyl phosphate


substrate_name: deoxy-ribose 1-phosphate

substrate: deoxy-ribose 1-phosphate


substrate_name: 2-deoxy-D-ribose 1-phosphate

proof_lines: kcat is 173 sec(-1) (at 90 degrees Celsius).

substrate: 2-deoxy-D-ribose 1-phosphate


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: Unknown

substrate: Unknown


proof_lines: Glucose-1,6-bisphosphate is essential for activity.


substrate_name: D-Glucose 1,6-bisphosphate; D-Mannose 6-phosphate


organism: Plasmodium falciparum (isolate 3D7)

sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

proof_lines: kcat is 0.00017 sec(-1) for the conversion of mannose 6-phosphate (M6P) to mannose 1-phosphate (M1P) in the presence of glucose-1,6-bisphosphate (G-1,6-P) (at room temperature). kcat is 0.0000078 sec(-1) for the conversion of glucose 1-phos


organism: Tetrahymena pyriformis


substrate_name: N-Acetylglucosamine 6-phosphate

substrate: N-Acetylglucosamine 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D276E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H65R to reconstruct the assayed variant sequence.


substrate_name: beta-D-glucose 1-phosphate (using beta-D-glucose 1,6-(bis)phosphate as an activator, at pH 8.0, 30 degrees Celsius)

sequence_variant_note: Mutation signature G1P/G6P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: kcat is 21 sec(-1) for conversion of G1P to G6P, kcat is 0.5 sec(-1) for conversion of G6P to G1P.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D280A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D70A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G277A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G499A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G58A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G72A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K74A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N66A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P67A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R496A to reconstruct the assayed variant sequence.


substrate_name: mannose 6-phosphate (M6P) (at room temperature)


substrate_name: glucose 1-phosphate (G1P) (at room temperature)


sequence_variant_note: Mutation signature R498A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T500A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T62A to reconstruct the assayed variant sequence.


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


substrate_name: beta-D-Glucose 1,6-bisphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H20A to reconstruct the assayed variant sequence.

column_label: Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis H20A / betaG1,6bisP hydrolysis; column kcat (s^-1); metric kcat; normalized value 0.0197 s^-1 | Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis H20A / betaG1,6bisP hydrolysis; column Km (uM); metric km; normalized value 0.0026 mM | Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis H20A / betaG1,6bisP hydrolysis; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 7.5769230769230775 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.0197 normalized_unit=s^-1; km normalized_value=0.0026 normalized_unit=mM; kcat_over_km normalized_value=7.5769230769230775 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.0197 raw_unit=s^-1; km raw_value=2.6 raw_unit=uM; kcat_over_km raw_value=0.0197/0.0026 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells

substrate: beta-D-Glucose 1,6-bisphosphate


sequence_variant_note: Resolved canonical sequence from package_local_exact_accession:P71447 and applied mutation signature H20N to reconstruct the assayed variant sequence.

column_label: Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis H20N / betaG1,6bisP hydrolysis; column kcat (s^-1); metric kcat; normalized value 0.0303 s^-1 | Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis H20N / betaG1,6bisP hydrolysis; column Km (uM); metric km; normalized value 0.00149 mM | Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis H20N / betaG1,6bisP hydrolysis; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 20.335570469798657 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.0303 normalized_unit=s^-1; km normalized_value=0.00149 normalized_unit=mM; kcat_over_km normalized_value=20.335570469798657 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.0303 raw_unit=s^-1; km raw_value=1.49 raw_unit=uM; kcat_over_km raw_value=0.0303/0.00149 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T16P to reconstruct the assayed variant sequence.

column_label: Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis T16P / betaG1,6bisP hydrolysis; column kcat (s^-1); metric kcat; normalized value 0.38 s^-1 | Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis T16P / betaG1,6bisP hydrolysis; column Km (uM); metric km; normalized value 0.010 mM | Table 4. beta-PGM-catalyzed betaG1,6bisP hydrolysis kinetic constants; row L. lactis T16P / betaG1,6bisP hydrolysis; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 38.0 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.38 normalized_unit=s^-1; km normalized_value=0.010 normalized_unit=mM; kcat_over_km normalized_value=38.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.38 raw_unit=s^-1; km raw_value=10 raw_unit=uM; kcat_over_km raw_value=0.38/0.010 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells


substrate_name: beta-D-Glucose 1-phosphate

column_label: Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20A / betaG1P mutase reaction; column kcat (s^-1); metric kcat; normalized value 0.026 s^-1 | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20A / betaG1P mutase reaction; column Km (uM); metric km; normalized value 0.041 mM | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20A / betaG1P mutase reaction; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 0.6341463414634145 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.026 normalized_unit=s^-1; km normalized_value=0.041 normalized_unit=mM; kcat_over_km normalized_value=0.6341463414634145 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.026 raw_unit=s^-1; km raw_value=41 raw_unit=uM; kcat_over_km raw_value=0.026/0.041 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells

substrate: beta-D-Glucose 1-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P71447 and applied mutation signature H20N to reconstruct the assayed variant sequence.

column_label: Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20N / betaG1P mutase reaction; column kcat (s^-1); metric kcat; normalized value 0.62 s^-1 | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20N / betaG1P mutase reaction; column Km (uM); metric km; normalized value 0.170 mM | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20N / betaG1P mutase reaction; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 3.6470588235294117 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.62 normalized_unit=s^-1; km normalized_value=0.170 normalized_unit=mM; kcat_over_km normalized_value=3.6470588235294117 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.62 raw_unit=s^-1; km raw_value=170 raw_unit=uM; kcat_over_km raw_value=0.62/0.170 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P71447 and applied mutation signature H20Q to reconstruct the assayed variant sequence.

column_label: Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20Q / betaG1P mutase reaction; column kcat (s^-1); metric kcat; normalized value 21.9 s^-1 | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20Q / betaG1P mutase reaction; column Km (uM); metric km; normalized value 0.045 mM | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis H20Q / betaG1P mutase reaction; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 486.66666666666663 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=21.9 normalized_unit=s^-1; km normalized_value=0.045 normalized_unit=mM; kcat_over_km normalized_value=486.66666666666663 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=21.9 raw_unit=s^-1; km raw_value=45 raw_unit=uM; kcat_over_km raw_value=21.9/0.045 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K76A to reconstruct the assayed variant sequence.

column_label: Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis K76A / betaG1P mutase reaction; column kcat (s^-1); metric kcat; normalized value 1.56 s^-1 | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis K76A / betaG1P mutase reaction; column Km (uM); metric km; normalized value 0.066 mM | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis K76A / betaG1P mutase reaction; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 23.636363636363637 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=1.56 normalized_unit=s^-1; km normalized_value=0.066 normalized_unit=mM; kcat_over_km normalized_value=23.636363636363637 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.56 raw_unit=s^-1; km raw_value=66 raw_unit=uM; kcat_over_km raw_value=1.56/0.066 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells


column_label: Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis T16P / betaG1P mutase reaction; column kcat (s^-1); metric kcat; normalized value 0.026 s^-1 | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis T16P / betaG1P mutase reaction; column Km (uM); metric km; normalized value 0.0048 mM | Table 2. Steady state kinetic constants for wild type and mutant beta-PGM; row L. lactis T16P / betaG1P mutase reaction; column Computed from exact kcat and Km cells; metric kcat_over_km; normalized value 5.416666666666667 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.026 normalized_unit=s^-1; km normalized_value=0.0048 normalized_unit=mM; kcat_over_km normalized_value=5.416666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.026 raw_unit=s^-1; km raw_value=4.8 raw_unit=uM; kcat_over_km raw_value=0.026/0.0048 raw_unit=s^-1*mM^-1; computed from explicit kcat and Km cells


proof_lines:
Raw SKiD Env: Temp=25°C, pH=6.5
Raw SKiD Env: Temp=32°C, pH=7.5


substrate_name: alpha-D-Mannose 1-phosphate

substrate: alpha-D-Mannose 1-phosphate


substrate_name: D-glucosamine 1-phosphate

substrate: D-glucosamine 1-phosphate


substrate_name: D-glucose 1-phosphate

substrate: D-glucose 1-phosphate


substrate_name: fructose 1,6-diphosphate

substrate: fructose 1,6-diphosphate


substrate_name: glucose 1,6-diphosphate

substrate: glucose 1,6-diphosphate


organism: Galdieria sulphuraria

proof_lines: Glucose-1,6-bisphosphate or mannose-1,6-biphosphate are essential for activity.


organism: Saccharomyces cerevisiae

substrate_name: D-Ribose 1-phosphate

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

column_label: Table 3 row Pgm3 under ribose-1-phosphate has Vmax, km, and kcat/km columns; values are 0.29, 750, and 0.46 respectively

raw_value_unit_evidence: Ribose-1-phosphate columns report Vmax=0.29 +/- 0.06 umol/(min mgprot), km=750 +/- 35 uM, kcat/km=0.46

row_label: Pgm3 / ribose-1-phosphate

substrate: D-Ribose 1-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G46A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature G46P could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature G46V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K45A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K45R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R49A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S52A to reconstruct the assayed variant sequence.


substrate_name: beta-D-glucose 1,6-(bis)phosphate

sequence_variant_note: Mutation signature G1P/G6P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: beta-D-glucose 1,6-(bis)phosphate


organism: Mytilus edulis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L124A to reconstruct the assayed variant sequence.

proof_lines:
mutant L124A, pH 7.5, 25°C
mutant enzyme L124A, at pH 7.5 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K120R to reconstruct the assayed variant sequence.

proof_lines:
mutant K120R, pH 7.5, 25°C
mutant enzyme K120R, at pH 7.5 and 25°C


substrate_name: Phosphonopyruvate

mutation_signature: truncated enzyme truncated enzyme

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

mutation_type: truncation

substrate: Phosphonopyruvate


mutation_signature: truncated enzyme


substrate_name: 2-Deoxy-D-ribose 1-phosphate

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

substrate: 2-Deoxy-D-ribose 1-phosphate


substrate_name: Ribose 1-phosphate

substrate: Ribose 1-phosphate


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


substrate_name: 2-deoxyribose 1-phosphate

substrate: 2-deoxyribose 1-phosphate


proof_lines: GlmM was also capable of catalysing the interconversion of glucose-1-phosphate and glucose-6-phosphate isomers


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Triticum aestivum

substrate_name: alpha-D-mannose 1-phosphate

proof_lines: isoform PMM-D1, 30°C, pH not specified in the publication

proof_lines: isoform PMM-A1, 37°C, pH not specified in the publication

proof_lines: isoform PMM-D2, 30°C, pH not specified in the publication

substrate: alpha-D-mannose 1-phosphate


organism: Escherichia coli

substrate_name: D-Glucosamine 1-phosphate

proof_lines: GlmM interconverts glucosamine-6-phosphate and glucosamine-1-phosphate

substrate: D-Glucosamine 1-phosphate


substrate_name: D-Glucosamine 6-phosphate

substrate: D-Glucosamine 6-phosphate


substrate_name: beta-D-Glucose 1-phosphate

proof_lines: GlmM also catalyzes glucose-1-phosphate and glucose-6-phosphate isomerization

substrate: beta-D-Glucose 1-phosphate


substrate_name: Glucosamine 1,6-diphosphate

proof_lines: GlcN-1,6-diphosphate intermediate in the GlmM mechanism

substrate: Glucosamine 1,6-diphosphate


substrate_name: Glucose 1,6-diphosphate

proof_lines: Glc-1,6-diphosphate-dependent low-activity phosphoglucomutase activity

substrate: Glucose 1,6-diphosphate


substrate_name: 4-Nitrophenyl phosphate

normalized_value_unit_evidence: kcat: printed (1.78 ( 0.01) × 10-2 s-1 is (1.78 +/- 0.01) x 10^-2 s^-1 = 0.0178 s^(-1); the export stores kcat at three decimal places, and 0.0178 rounds to the stored 0.018 s^(-1), a precision-only difference. Km: printed 14.3 ( 0.3 mM is 14.3 +/- 0.3 mM = 14.3 mM exactly as stored. kcat/Km: the paper prints no efficiency ratio for pNPP; the export value is the quotient of the export-stored kcat and the printed Km, 0.018 s^-1 / 14.3 mM = 0.0012587412587412585 s^-1 mM^-1. The same quotient computed from the fully printed kcat, 0.0178 / 14.3 = 0.0012447552447552448 s^-1 mM^-1, agrees with it once the kcat is taken at the export's stored precision; the gap is printed precision only. OCR quirks: ) renders =, ( renders +/-, × 10-2 is x 10^-2, s-1 is s^-1.

raw_value_unit_evidence: Results sentence on p 9413 (section: Specificity of Phospho-beta-PGM for the Phosphoryl Group Acceptor): the steady-state constants measured using 2 uM beta-PGM in 2 mM MgCl2 and 50 mM K+Hepes (pH 7.0 and 25 C) read kcat = (1.78 +/- 0.01) x 10^-2 s^-1 and pNPP Km = 14.3 +/- 0.3 mM. In the OCR text the sentence is split across the two right-column lines `follows: kcat ) (1.78 ( 0.01) × 10-2 s-1 and pNPP Km )` and `14.3 ( 0.3 mM.`, interleaved with the left-column line `phosphatase because of its ability to discriminate between`. The BT4131 values printed directly after (kcat 8.3 x 10-2 s-1, Km 0.77 mM) belong to the different enzyme BT4131 at 37 C and are not used.

substrate: 4-Nitrophenyl phosphate


substrate_name: Acetyl phosphate

smiles: CC(=O)OP(=O)(O)O

normalized_value_unit_evidence: kcat: printed 16.6 ( 0.3 s-1 is 16.6 +/- 0.3 s^-1 = 16.6 s^(-1) exactly as stored. Km: printed 800 ( 30 µM is 800 +/- 30 uM = 0.8 mM (1 uM = 0.001 mM), exactly as stored. kcat/Km: the paper prints no efficiency ratio for acetyl phosphate; the export value is the quotient of this sentence's own printed values, 16.6 s^-1 / 0.8 mM = 20.75 s^-1 mM^-1. OCR quirks: ) renders =, ( renders +/-, s-1 is s^-1, µM is uM.

raw_value_unit_evidence: Results sentence on p 9412 (Figure 6C context): the steady-state kinetic constants for acetyl phosphate read kcat = 16.6 +/- 0.3 s^-1 and Km = 800 +/- 30 uM. In the OCR text the sentence spans the two right-column lines `the steady-state kinetic constants (kcat ) 16.6 ( 0.3 s-1 and` and `Km ) 800 ( 30 µM) for acetyl phosphate were derived from`, interleaved with the left-column line `illustrated by the kinetic plot measured with R-G16P (Figure`.

substrate: Acetyl phosphate


substrate_name: alpha-D-Glucose 1,6-bisphosphate

normalized_value_unit_evidence: kcat: Table 2 wild-type cell 17.1 ( 0.6 is 17.1 +/- 0.6 s^-1 = 17.1 s^(-1) exactly as stored; the Figure 6A prose prints the same turnover as 17 s^-1 at its own two-figure precision. Km: printed `a Km of 20 µM ... for the activator R-G16P` is 20 uM = 0.02 mM (1 uM = 0.001 mM), exactly as stored. kcat/Km: the paper prints no efficiency ratio for R-G16P; the export value is the quotient 17.1 s^-1 / 0.02 mM = 855.0 s^-1 mM^-1. OCR quirks: R- renders the Greek alpha (R-G16P is alpha-D-glucose 1,6-bisphosphate, defined in the abbreviations footnote), ( renders +/-, s-1 is s^-1, µM is uM; the prose segment interleaves the right-column line `a separate set of initial velocity data measured over a range` between the two left-column fragments.

raw_value_unit_evidence: Two mutually consistent printed locations for the same wild-type R-G16P-activated measurement context. (1) Results prose, Figure 6A bi-bi ping-pong fit: `Data fitting defined a kcat of 17 s-1 and a Km of 20 µM` ... `for the activator R-G16P.` - Km for the activator R-G16P = 20 uM and kcat = 17 s^-1. (2) Table 2: Kinetic Constants for Wild-Type and Mutant beta-PGMs (in the presence of 50 uM R-G16P as the activator), header `enzyme Km-Mg2+ (µM) Km-G1P (µM) kcat (s-1)`, row `wild type 270 ( 20 14.6 ( 0.5 17.1 ( 0.6` - the wild-type kcat cell reads 17.1 +/- 0.6 s^-1. The exported kcat is the Table 2 cell 17.1 s^-1; the prose kcat 17 s^-1 is the same turnover number printed at two significant figures.

row_label: wild type

table_label: Table 2: Kinetic Constants for Wild-Type and Mutant β-PGMs (in the presence of 50 µM R-G16P as the activator)

substrate: alpha-D-Glucose 1,6-bisphosphate


normalized_value_unit_evidence: Km: Table 2 wild-type Km-Mg2+ cell 270 ( 20 is 270 +/- 20 uM = 0.27 mM (1 uM = 0.001 mM), exactly as stored. kcat: Table 2 wild-type kcat cell 17.1 ( 0.6 is 17.1 +/- 0.6 s^-1 = 17.1 s^(-1), exactly as stored. kcat/Km: the paper prints no efficiency ratio for Mg2+ activation; the export value is the quotient of this row's own printed cells, 17.1 s^-1 / 0.27 mM = 63.333333333333336 s^-1 mM^-1. OCR quirks: ( renders +/-, s-1 is s^-1, µM is uM.

raw_value_unit_evidence: Table 2: Kinetic Constants for Wild-Type and Mutant beta-PGMs (in the presence of 50 uM R-G16P as the activator) | header row: `enzyme Km-Mg2+ (µM) Km-G1P (µM) kcat (s-1)` | row: `wild type 270 ( 20 14.6 ( 0.5 17.1 ( 0.6` | wild-type cells read: Km-Mg2+ = 270 +/- 20 uM; Km-G1P = 14.6 +/- 0.5 uM; kcat = 17.1 +/- 0.6 s^-1. Corroborating Results prose (Figure 5): `apparent Km for Mg2+ of 270 ( 20 µM` - an apparent Km for Mg2+ of 270 +/- 20 uM.


organism: Lactococcus lactis subsp. lactis (strain IL1403)

substrate_name: alpha-D-glucose 1,6-bisphosphate (at pH 7 and 25 degrees Celsius)


substrate_name: magnesium (at pH 7 and 25 degrees Celsius)

smiles: [Mg]


substrate_name: acetyl-phosphate (at pH 7 and 25 degrees Celsius)


organism: Pseudomonas aeruginosa

substrate_name: D-Mannose 1-phosphate

proof_lines: kcat is 3000 min(-1) for glucose 1-phosphate and 1350 min(-1) for mannose 1-phosphate.

substrate: D-Mannose 1-phosphate


substrate_name: Glycerate 1,3-bisphosphate

substrate: Glycerate 1,3-bisphosphate


organism: Homo sapiens

substrate_name: alpha-D-Ribose 1-phosphate

substrate: alpha-D-Ribose 1-phosphate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: glucose 1-phosphate

substrate: glucose 1-phosphate


column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjU / beta-D-glucose-1-P; fixed substrate none; columns kcat column raw 21 +/- 1 normalized 21 s^-1; Km column raw 0.018 +/- 0.001 normalized 0.018 mM; kcat/Km column raw (1.1 +/- 0.1) x 10^6 M^-1 s^-1 normalized from same-row kcat and Km as 1166.6666666666667 s^-1*mM^-1; export values for required/current metrics match these normalized values.

normalized_value_unit_evidence: kcat normalized_value=21 normalized_unit=s^-1; Km normalized_value=0.018 normalized_unit=mM; kcat/Km normalized_value=1166.6666666666667 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=(1.1 +/- 0.1) x 10^6 M^-1 s^-1

raw_value_unit_evidence: kcat raw_value=21 +/- 1 raw_unit=s^-1; Km raw_value=0.018 +/- 0.001 raw_unit=mM; kcat/Km raw_value=(1.1 +/- 0.1) x 10^6 M^-1 s^-1 raw_unit=M^-1 s^-1


substrate_name: D-Glucose 6-phosphate

column_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C; row YcjU / D-glucose-6-P; fixed substrate none; columns kcat column raw 0.5 +/- 0.1 normalized 0.5 s^-1; Km column raw 1.19 +/- 0.04 normalized 1.19 mM; kcat/Km column raw (4.2 +/- 0.1) x 10^2 M^-1 s^-1 normalized from same-row kcat and Km as 0.42016806722689076 s^-1*mM^-1; export values for required/current metrics match these normalized values.

normalized_value_unit_evidence: kcat normalized_value=0.5 normalized_unit=s^-1; Km normalized_value=1.1900000000000002 normalized_unit=mM; kcat/Km normalized_value=0.4201680672268907 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=(4.2 +/- 0.1) x 10^2 M^-1 s^-1

raw_value_unit_evidence: kcat raw_value=0.5 +/- 0.1 raw_unit=s^-1; Km raw_value=1.19 +/- 0.04 raw_unit=mM; kcat/Km raw_value=(4.2 +/- 0.1) x 10^2 M^-1 s^-1 raw_unit=M^-1 s^-1

substrate: D-Glucose 6-phosphate


substrate_name: beta-D-Allose 1-phosphate

substrate: beta-D-Allose 1-phosphate


substrate_name: beta-D-glucose 1-phosphate

substrate: beta-D-glucose 1-phosphate


substrate_name: beta-D-glucose 6-phosphate

normalized_value_unit_evidence: kcat normalized_value=0.5 normalized_unit=s^-1; Km normalized_value=1.19 normalized_unit=mM; kcat/Km normalized_value=0.42016806722689076 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=(4.2 +/- 0.1) x 10^2 M^-1 s^-1

row_label: YcjU / D-glucose-6-P; fixed substrate none

table_label: Table 1. Apparent kinetic constants for YcjM (pH 6.5), YcjT (pH 7.5), and YcjU (pH 8.0) at 30 C

substrate: beta-D-glucose 6-phosphate


organism: Escherichia coli (strain K12)

substrate_name: ribose 1-phosphate

substrate: ribose 1-phosphate


organism: Thermotoga maritima

substrate_name: alpha-D-ribose 5-phosphate

proof_lines:
at pH 7.5 and 60°C
at pH 7.5 and 90°C

substrate: alpha-D-ribose 5-phosphate


organism: Gallus gallus


organism: Lactococcus lactis subsp. lactis

substrate_name: beta-D-Glucose 1,6-bisphosphate

substrate: beta-D-Glucose 1,6-bisphosphate


substrate_name: D-glucose 1-phosphate

substrate: D-glucose 1-phosphate


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


proof_lines:
R247A mutant
mutant R247A


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


substrate_name: D-Ribose 1-phosphate

substrate: D-Ribose 1-phosphate


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


substrate_name: Unknown

proof_lines:
at pH 7.0 and 25°C
Ki about 0.2 mM, at pH 7.0 and 25°C

substrate: Unknown


substrate_name: Ribose 5-phosphate

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

substrate: Ribose 5-phosphate


substrate_name: phosphoenolpyruvate

column_label: Abstract states PEP mutase catalyzed conversion of PEP to P-pyr at pH 7.5 and 25 degrees C has Km = 0.77 +/- 0.05 mM.

raw_value_unit_evidence: Km raw_value=0.77 +/- 0.05 raw_unit=mM

row_label: Tetrahymena pyriformis PEP mutase with phosphoenolpyruvate

table_label: PubMed abstract PMID 8605214

substrate: phosphoenolpyruvate


proof_lines: mutant enzyme E325A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4


proof_lines: mutant enzyme Y17A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4


proof_lines: mutant enzyme R262A/P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4


proof_lines: mutant enzyme R262A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4


proof_lines: mutant enzyme P368A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4


proof_lines: mutant enzyme P368G, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4


proof_lines: mutant enzyme S369A, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4


proof_lines: wild type enzyme, at 25°C in 50 mM MOPS (pH 7.4) with 1 mM dithiothreitol, 1.5 mM MgSO4


proof_lines:
single-mutation S100T
single mutation S100T


substrate_name: D-glucosamine 6-phosphate

substrate: D-glucosamine 6-phosphate


substrate_name: D-glucosamine 1-phosphate

substrate: D-glucosamine 1-phosphate


substrate_name: D-glucosamine 1,6-diphosphate

substrate: D-glucosamine 1,6-diphosphate


substrate_name: D-Glucose 1,6-bisphosphate

substrate: D-Glucose 1,6-bisphosphate


substrate_name: beta-D-Glucose 1-phosphate

substrate: beta-D-Glucose 1-phosphate


organism: Mus musculus

substrate_name: glucose-1,6-bisphosphate in the presence of 1 uM IMP


organism: Aspergillus fumigatus


substrate_name: alpha-D-mannose 1-phosphate

substrate: alpha-D-mannose 1-phosphate


substrate_name: beta-D-glucose 6-phosphate


substrate_name: beta-D-glucose 1-phosphate

substrate: beta-D-glucose 1-phosphate


organism: Arabidopsis thaliana

proof_lines:
mutant enzyme G7R/R37Q, at 18°C
mutant enzyme G7R/R37Q, at 28°C


proof_lines:
mutant enzyme R37Q, at 18°C
mutant enzyme R37Q, at 28°C


proof_lines:
wild type enzyme, at 18°C
wild type enzyme, at 28°C


proof_lines:
mutant enzyme G7R, at 18°C
mutant enzyme G7R, at 28°C


enzyme_display_name: selenocysteine lyase

organism: Citrobacter freundii

substrate_name: L-selenocysteine

smiles: C(C(C(=O)O)N)[SeH]

enzyme: selenocysteine lyase

substrate: L-selenocysteine


substrate_name: beta-chloro-L-alanine

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

substrate: beta-chloro-L-alanine


organism: Zea mays

substrate_name: D-Glucose 1-phosphate

proof_lines: 25°C, pH 7.6, substrate inhibition at high concentrations

substrate: D-Glucose 1-phosphate


substrate_name: alpha-D-Glucose 1,6-bisphosphate

substrate: alpha-D-Glucose 1,6-bisphosphate


substrate_name: D-Mannose 1-phosphate

substrate: D-Mannose 1-phosphate


proof_lines: wild-type, heterodimer, room temperature


proof_lines:
mutant enzyme R159A, at pH 7.5 and 25°C
mutant R159A, 25°C, pH 7.5


proof_lines:
mutant enzyme H190A, at pH 7.5 and 25°C
mutant H190A, 25°C, pH 7.5


proof_lines:
mutant enzyme N122D, at pH 7.5 and 25°C
mutant N122D, 25°C, pH 7.5


proof_lines:
wild type enzyme, at pH 7.5 and 25°C
wild-type, pH 7.5, 25°C


substrate_name: poly(A)poly(U)

proof_lines:
ADA mutant
PE3 variant, pH 5.5, 25°C
PE3I2 variant, pH 5.5, 25°C

substrate: poly(A)poly(U)


organism: Lactococcus lactis


enzyme_display_name: prostaglandin-E synthase

substrate_name: prostaglandin H2

enzyme: prostaglandin-E synthase

substrate: prostaglandin H2


enzyme_display_name: dichloromethane dehalogenase

organism: Hyphomicrobium sp.

substrate_name: Diiodomethane

smiles: C(I)I

enzyme: dichloromethane dehalogenase

substrate: Diiodomethane


substrate_name: Dibromomethane

smiles: C(Br)Br

substrate: Dibromomethane


organism: Malus domestica

substrate_name: S-methyl-L-methionine

smiles: C[S+](C)CCC(C(=O)O)N

substrate: S-methyl-L-methionine


substrate_name: L-alanine

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

substrate: L-alanine


substrate_name: L-Vinylglycine

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

proof_lines:
inactivation
deamination
alpha-ketobutyrate production

substrate: L-Vinylglycine


enzyme_display_name: leukotriene-C4 synthase

substrate_name: leukotriene A4

proof_lines: pH 7.8, temperature not specified in the publication, recombinant enzyme

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4


substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

substrate: glutathione


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: UniProt Q86N96

organism: Leishmania mexicana

enzyme: UniProt Q86N96


enzyme_display_name: L-lysine 2,3-aminomutase

organism: Bacillus subtilis (strain 168)

substrate_name: L-lysine

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

enzyme: L-lysine 2,3-aminomutase

substrate: L-lysine


enzyme_display_name: UniProt E3PY96

organism: Acetoanaerobium sticklandii

substrate_name: D-ornithine

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

enzyme: UniProt E3PY96

substrate: D-ornithine


enzyme_display_name: methionine gamma-lyase

substrate_name: L-cystathionine

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

enzyme: methionine gamma-lyase

substrate: L-cystathionine


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: L-methionine

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

substrate: L-methionine


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Pseudomonas sp. 'cruciviae'

substrate_name: pyridoxal phosphate

enzyme: cysteine-S-conjugate beta-lyase

substrate: pyridoxal phosphate


substrate_name: S-methyl-L-cysteine

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

substrate: S-methyl-L-cysteine


substrate_name: S-methyl-L-cysteine sulfoxide

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

substrate: S-methyl-L-cysteine sulfoxide


organism: Pseudomonas putida

substrate_name: Se-methyl-L-selenocysteine

smiles: C[Se]CC(C(=O)O)N

substrate: Se-methyl-L-selenocysteine


substrate_name: O-methyl-L-serine

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

substrate: O-methyl-L-serine


organism: Rattus norvegicus

proof_lines: mitochondria cytoplasm


substrate_name: beta-chloroalanine

substrate: beta-chloroalanine


substrate_name: protoporphyrin IX

proof_lines: mutant enzyme F283L, at pH 8.0, temperature not specified in the publication

substrate: protoporphyrin IX


proof_lines: mutant enzyme H287L, at pH 8.0, temperature not specified in the publication


organism: Sus scrofa

substrate_name: Glycerate 3-phosphate

proof_lines:
MB-type and BB-type isozymes
MM-type isozyme

substrate: Glycerate 3-phosphate


enzyme_display_name: lysine 5,6-aminomutase

organism: Porphyromonas gingivalis

substrate_name: (S)-lysine

proof_lines: pH and temperature not specified in the publication

enzyme: lysine 5,6-aminomutase

substrate: (S)-lysine


substrate_name: (S)-beta-lysine

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

substrate: (S)-beta-lysine


organism: Plasmodium falciparum


organism: Zymomonas mobilis


substrate_name: L-homoserine

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

substrate: L-homoserine


substrate_name: DL-homocysteine

substrate: DL-homocysteine


organism: Tetrahymena pyriformis

substrate_name: Phosphonopyruvate

substrate: Phosphonopyruvate


enzyme_display_name: D-ornithine 4,5-aminomutase

substrate_name: D-ornithine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H225A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

enzyme: D-ornithine 4,5-aminomutase

substrate: D-ornithine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H225Q with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature E81A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 298.15 K; buffer and pH stated in its Fig

column_label: Table 1: Summary of steady-state kinetic parameters for OAM and its active site variants with substrate D-ornithine and inhibitor 2,4-diaminobutyrate (BBA - Proteins and Proteomics 2017, 1865:1077-1084); Enzyme row 'E81A': column 'kcat (s-1)' = 0.013; column 'Km (uM)' = 780; column 'kcat/Km x 103 (s-1 M-1)' = 0.016; column 'Ki (DABA) (uM)' = ND. The efficiency column is printed in units of 10^3 s-1 M-1, which is the same size as 1 s-1 mM-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.013 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.013 s^(-1); the exported value is 0.013 s^(-1). Km: printed Table 1 cell 780 uM; 780 / 1000 = 0.78 mM; the exported value is 0.78 mM. kcat/Km: printed Table 1 cell 0.016 in units of 10^3 s-1 M-1, that is 16 s-1 M-1; 1 s-1 M-1 is 0.001 s-1 mM-1, so the printed cell becomes 0.016 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.013 / 0.78 = 0.016666666666666666 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Enzyme row 'E81A': kcat = 0.013 s-1; Km = 780 uM; printed kcat/Km = 0.016 in the column's units of 10^3 s-1 M-1.

row_label: Table 1, Enzyme row 'E81A', the printed kcat, Km and kcat/Km cells of that row


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


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:E3PY95 and applied mutation signature Y160F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; buffer and pH stated in its Fig

column_label: Table 1: Summary of steady-state kinetic parameters for OAM and its active site variants with substrate D-ornithine and inhibitor 2,4-diaminobutyrate (BBA - Proteins and Proteomics 2017, 1865:1077-1084); Enzyme row 'Y160F': column 'kcat (s-1)' = 0.027; column 'Km (uM)' = 140; column 'kcat/Km x 103 (s-1 M-1)' = 0.19; column 'Ki (DABA) (uM)' = 2000 uM. The efficiency column is printed in units of 10^3 s-1 M-1, which is the same size as 1 s-1 mM-1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.027 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.027 s^(-1); the exported value is 0.027 s^(-1). Km: printed Table 1 cell 140 uM; 140 / 1000 = 0.14 mM; the exported value is 0.14 mM. kcat/Km: printed Table 1 cell 0.19 in units of 10^3 s-1 M-1, that is 190 s-1 M-1; 1 s-1 M-1 is 0.001 s-1 mM-1, so the printed cell becomes 0.19 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed component cells is 0.027 / 0.14 = 0.19285714285714284 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, Enzyme row 'Y160F': kcat = 0.027 s-1; Km = 140 uM; printed kcat/Km = 0.19 in the column's units of 10^3 s-1 M-1.

row_label: Table 1, Enzyme row 'Y160F', the printed kcat, Km and kcat/Km cells of that row