Information on EC 4.1.2.14 - 2-dehydro-3-deoxy-phosphogluconate aldolase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY
4.1.2.14
-
RECOMMENDED NAME
GeneOntology No.
2-dehydro-3-deoxy-phosphogluconate aldolase
PATHWAY
KEGG Link
MetaCyc Link
5-dehydro-4-deoxy-D-glucuronate degradation
-
D-fructuronate degradation
-
D-glucosaminate degradation
-
Entner-Doudoroff pathway I
-
Entner-Doudoroff pathway III (semi-phosphorylative)
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
SYSTEMATIC NAME
IUBMB Comments
2-dehydro-3-deoxy-6-phosphate-D-gluconate D-glyceraldehyde-3-phosphate-lyase (pyruvate-forming)
The enzyme shows no activity with 2-dehydro-3-deoxy-6-phosphate-D-galactonate. cf. EC 4.1.2.55, 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase [2]. Also acts on 2-oxobutanoate [1].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-dehydro-3-deoxyphosphogluconate aldolase
-
-
-
-
2-keto-3-deoxy-(6-phospho)-gluconate aldolase
-
-
2-keto-3-deoxy-(6-phospho)-gluconate aldolase
Q704D1
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
A4VVI7
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
-
-
2-keto-3-deoxy-6-phosphogluconate aldolase
Zymomonas mobilis ZM4
-
-
-
2-keto-3-deoxy-6-phosphogluconic aldolase
-
-
-
-
2-keto-3-deoxygluconate-6-P-aldolase
-
-
-
-
2-keto-3-deoxygluconate-6-phosphate aldolase
-
-
-
-
2-oxo-3-deoxy-6-phosphogluconate aldolase
-
-
-
-
6-phospho-2-dehydro-3-deoxy-D-gluconate D-glyceraldehyde-3-phosphate-lyase
-
-
-
-
6-Phospho-2-keto-3-deoxygluconate aldolase
-
-
-
-
aldolase, phospho-2-keto-3-deoxygluconate
-
-
-
-
KD(P)G aldolase
-
-
KD(P)G aldolase
Q704D1
-
KDPG aldolase
-
-
-
-
KDPG aldolase
A4VVI7
-
KDPG aldolase
-
-
KDPG aldolase
-
-
KDPG aldolase
Zymomonas mobilis ZM4
-
-
-
KDPG-aldolase
-
-
-
-
ODPG aldolase
-
-
-
-
Phospho-2-dehydro-3-deoxygluconate aldolase
-
-
-
-
Phospho-2-keto-3-deoxygluconate aldolase
-
-
-
-
Phospho-2-keto-3-deoxygluconic aldolase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-53-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain Lhet2, strain PW2, strain KLB, strain OP and strain QBP
-
-
Manually annotated by BRENDA team
bifunctional enzyme Ec4.1.2.14/Ec4.1.3.16
-
-
Manually annotated by BRENDA team
strain CC409
-
-
Manually annotated by BRENDA team
Bradyrhizobium japonicum CC409
strain CC409
-
-
Manually annotated by BRENDA team
strain H16
-
-
Manually annotated by BRENDA team
a L-lysine producer of Methylophilus methylotrophus is constructed by the introduction of the Escherichia coli edd-eda operon
-
-
Manually annotated by BRENDA team
strain NZP2213
-
-
Manually annotated by BRENDA team
Mesorhizobium loti NZP2213
strain NZP2213
-
-
Manually annotated by BRENDA team
strain A 3.12
-
-
Manually annotated by BRENDA team
Pelomonas saccharophila A 3.12
strain A 3.12
-
-
Manually annotated by BRENDA team
strain CC224; strain SU391
-
-
Manually annotated by BRENDA team
Rhizobium leguminosarum CC224
strain CC224
-
-
Manually annotated by BRENDA team
Rhizobium leguminosarum SU391
strain SU391
-
-
Manually annotated by BRENDA team
strain RL3001
-
-
Manually annotated by BRENDA team
Rhizobium lupini RL3001
strain RL3001
-
-
Manually annotated by BRENDA team
strain CC365
-
-
Manually annotated by BRENDA team
Rhizobium phaseoli CC365
strain CC365
-
-
Manually annotated by BRENDA team
strain SU216
-
-
Manually annotated by BRENDA team
Sinorhizobium meliloti SU216
strain SU216
-
-
Manually annotated by BRENDA team
serotype 2
UniProt
Manually annotated by BRENDA team
strain ZM4
-
-
Manually annotated by BRENDA team
Zymomonas mobilis ZM4
strain ZM4
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
the eda gene disrupted mutant exhibits no appreciable change in growth characteristics in vitro, but is defective in multiplication within eukaryotic cells
malfunction
Legionella pneumophila AM511
-
the eda gene disrupted mutant exhibits no appreciable change in growth characteristics in vitro, but is defective in multiplication within eukaryotic cells
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
activates
Mg2+
-
activates
Mn2+
-
activates
Ni2+
-
activates
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.07
-
2,4-dioxo-4-phenylbutanoic acid
-
pH 7.6, 25C
0.04
-
2,4-dioxo-4-[2-(trifluoromethyl)phenyl]butanoic acid
-
pH 7.6, 25C
0.03
-
2,4-dioxo-4-[3-(trifluoromethyl)phenyl]butanoic acid
-
pH 7.6, 25C
0.38
-
2,4-dioxo-4-[4-(trifluoromethyl)phenyl]butanoic acid
-
pH 7.6, 25C
0.075
-
4-(3-methoxyphenyl)-2,4-dioxobutanoic acid
-
pH 7.6, 25C
0.18
-
4-(4-methoxyphenyl)-2,4-dioxobutanoic acid
-
pH 7.6, 25C
0.25
-
acetylpyruvic acid
-
pH 7.6, 25C
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Vibrio fischeri (strain ATCC 700601 / ES114)
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
-
-
4 h, stable
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E9K/V118A
-
KA1-4 variant, improved cleavage of D-2-dehydro-deoxygluconate
G40A/V188A
-
KA1-1 variant, improved cleavage of D-2-dehydro-deoxygluconate
K133Q
-
no aldolase activity
K133Q/T161K
-
reduced catalytic efficiency
S184A
-
the mutation decreases the efficiency of KDPG retro-aldol cleavage only modestly
S184D
-
the mutation leads to strongly reduced enzymatic activity
S184L
-
the mutation is located in the substrate-binding pocket, interacts with the phosphate moiety of KDPG, and improves the catalytic efficiency for the synthesis of a precursor for nikkomycin by 40fold
T161A
-
strongly reduced activity
T161V
-
strongly reduced activity
T84A/I92F
-
KA1-2 variant, improved cleavage of D-2-dehydro-deoxygluconate
T84A/I92F/V118A
-
KA2 variant, improved kcat, Km and thermal stability
T84A/I92F/V118A/E138V
-
KA3 variant, small change of melting temperature
T84A/I92F/V118A/G141S/T105I
-
KA3-L2 variant, slightly less stable than wild-type
T84A/I92F/V118A/T161A
-
KA3-L1 variant, enhanced activity towards negatively charged glyoxylate and glyceraldehyde-3-phosphate
V118A
-
KA1-3 variant, improved cleavage of D-2-dehydro-deoxygluconate