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Information on EC 4.1.2.13 - fructose-bisphosphate aldolase and Organism(s) Sus scrofa

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.2 Aldehyde-lyases
                4.1.2.13 fructose-bisphosphate aldolase
IUBMB Comments
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
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Sus scrofa
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The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
Synonyms
aldolase, aldolase a, aldolase b, aldolase c, aldoa, fructose-1,6-bisphosphate aldolase, fructose-bisphosphate aldolase, aldob, fructose bisphosphate aldolase, fructose 1,6-bisphosphate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,6-Diphosphofructose aldolase
-
-
-
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37 kDa major allergen
-
-
-
-
41 kDa antigen
-
-
-
-
aldolase
-
-
-
-
aldolase, fructose diphosphate
-
-
-
-
ALDP
-
-
-
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Brain-type aldolase
-
-
-
-
CE1
-
-
-
-
CE2
-
-
-
-
Diphosphofructose aldolase
-
-
-
-
FBP aldolase
-
-
-
-
Fru-P2A
-
-
-
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Fructoaldolase
-
-
-
-
Fructose 1,6-bisphosphate aldolase
-
-
-
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Fructose 1,6-diphosphate aldolase
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-
-
-
Fructose 1-monophosphate aldolase
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-
-
-
Fructose 1-phosphate aldolase
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-
-
-
Fructose bisphosphate aldolase
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-
-
-
Fructose diphosphate aldolase
-
-
-
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Fructose-1,6-bisphosphate triosephosphate-lyase
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-
-
-
IgE-binding allergen
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-
-
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ketose 1-phosphate aldolase
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-
-
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Liver-type aldolase
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-
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Muscle-type aldolase
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-
-
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Phosphofructoaldolase
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-
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SMALDO
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-
-
-
zymohexase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
condensation
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase (glycerone-phosphate-forming)
Also acts on (3S,4R)-ketose 1-phosphates. The yeast and bacterial enzymes are zinc proteins. The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-52-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-fructose 1,6-bisphosphate
glycerone phosphate + D-glyceraldehyde 3-phosphate
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
D-fructose 1,6-bisphosphate
-
immobilized enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
-
soluble enzyme
7.5
-
immobilized enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
soluble enzyme
45
-
immobilized enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A4X1U5U2_PIG
434
0
46774
TrEMBL
other Location (Reliability: 4)
A0A4X1VHB8_PIG
364
0
39699
TrEMBL
other Location (Reliability: 2)
A0A8D1HN75_PIG
536
0
57457
TrEMBL
Secretory Pathway (Reliability: 4)
A0A286ZTA4_PIG
364
0
39699
TrEMBL
other Location (Reliability: 2)
A0A8D1WSD1_PIG
367
0
39700
TrEMBL
other Location (Reliability: 1)
A0A286ZWI1_PIG
364
0
39377
TrEMBL
other Location (Reliability: 1)
A0A287B8Z2_PIG
434
0
46847
TrEMBL
other Location (Reliability: 4)
A0A480U1U8_PIG
479
0
51388
TrEMBL
Secretory Pathway (Reliability: 4)
A0A4X1U602_PIG
362
0
39421
TrEMBL
other Location (Reliability: 1)
A0A4X1TSU2_PIG
364
0
39377
TrEMBL
other Location (Reliability: 1)
A0A8D1HM45_PIG
438
0
46970
TrEMBL
other Location (Reliability: 2)
A0A8D0XSC2_PIG
434
0
46847
TrEMBL
other Location (Reliability: 4)
F1RJ25_PIG
336
0
36216
TrEMBL
other Location (Reliability: 1)
A0A287A1V5_PIG
510
0
55384
TrEMBL
other Location (Reliability: 5)
Q6UV40_PIG
109
0
12034
TrEMBL
other Location (Reliability: 1)
A0A286ZYX8_PIG
368
0
39818
TrEMBL
other Location (Reliability: 1)
A0A287BFY0_PIG
532
0
57356
TrEMBL
other Location (Reliability: 2)
A0A4X1TPV9_PIG
434
0
46893
TrEMBL
other Location (Reliability: 2)
A0A8D0P7Z3_PIG
412
0
44542
TrEMBL
other Location (Reliability: 5)
A0A287B8F3_PIG
416
0
44999
TrEMBL
other Location (Reliability: 5)
A0A4X1VEP5_PIG
316
0
35099
TrEMBL
other Location (Reliability: 2)
A0A8D1JH07_PIG
407
0
44239
TrEMBL
other Location (Reliability: 3)
A0A4X1U350_PIG
459
0
49429
TrEMBL
other Location (Reliability: 2)
A0A8D0QDP4_PIG
366
0
40213
TrEMBL
other Location (Reliability: 2)
A0A8D0P8B7_PIG
417
0
45163
TrEMBL
other Location (Reliability: 5)
Q70PG6_PIG
38
0
4402
TrEMBL
other Location (Reliability: 1)
A0A8D1U670_PIG
217
0
23417
TrEMBL
other Location (Reliability: 3)
A0A8D1ARN0_PIG
434
0
46889
TrEMBL
other Location (Reliability: 2)
A0A8D1HKE7_PIG
368
0
39818
TrEMBL
other Location (Reliability: 1)
A0A4X1U0N5_PIG
416
0
44999
TrEMBL
other Location (Reliability: 5)
A0A8D1BHM4_PIG
356
1
38748
TrEMBL
other Location (Reliability: 1)
A0A4X1VFM7_PIG
341
0
37179
TrEMBL
other Location (Reliability: 2)
A0A480HA34_PIG
381
0
40842
TrEMBL
other Location (Reliability: 2)
A0A480UEC6_PIG
405
0
43736
TrEMBL
other Location (Reliability: 5)
A0A286ZZC9_PIG
348
0
38041
TrEMBL
other Location (Reliability: 2)
A0A8D1JBH7_PIG
431
0
46822
TrEMBL
other Location (Reliability: 4)
A0A8D0PD98_PIG
439
0
47134
TrEMBL
other Location (Reliability: 2)
A0A8D1H065_PIG
348
0
38041
TrEMBL
other Location (Reliability: 2)
Q6UV41_PIG
40
0
4157
TrEMBL
other Location (Reliability: 1)
Q6UV39_PIG
66
0
6909
TrEMBL
other Location (Reliability: 2)
A0A4X1TSJ1_PIG
336
0
36216
TrEMBL
other Location (Reliability: 1)
A0A5G2RHD6_PIG
366
0
40213
TrEMBL
other Location (Reliability: 2)
Q29573_PIG
132
0
14657
TrEMBL
other Location (Reliability: 2)
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
maximal thermal stability in the pH-range, soluble enzyme
4932
7 - 7.5
-
maximal thermal stability in the pH-range, immobilized enzyme
4932
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
about 10% loss of activity of soluble enzyme and immobilized enzyme after 100 min
65
-
complete inactivation of the soluble enzyme after 40 min, complete inactivation of the immobilized enzyme after 70 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at 1-4 M urea, slight decrease in activity of the immobilized enzyme. In 5 M urea significant decrease in activity after 2 h. In 3 M urea the soluble enzyme unfolded and dissociated totally during 2 h
-
immobilization by covalent attachment to a polyacrylamide matrix containing carboxylic functional groups increases stability
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Abraham, M.; Horvath, L.; Simon, M.; Szajani, B.; Boross, L.
Characterization and comparison of soluble and immobilized pig muscle aldolases
Appl. Biochem. Biotechnol.
11
91-100
1985
Sus scrofa
Manually annotated by BRENDA team