EC number:4.1.2.42

Enzyme

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EC Tree
     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.2 Aldehyde-lyases
ID:4.1.2.42
Description:D-threonine aldolase.
Alternative Name: Low specificity D-threonine aldolase.
DTA.
Cath: 3.20.20.10; 2.40.37.20;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.2.42
BRENDA Enzyme Link: BRENDA 4.1.2.42
KEGG Enzyme Link: KEGG4.1.2.42
BioCyc Enzyme Link: BioCyc 4.1.2.42
ExPASy Enzyme Link: ExPASy4.1.2.42
EC2PDB Enzyme Link: EC2PDB 4.1.2.42
ExplorEnz Enzyme Link: ExplorEnz 4.1.2.42
PRIAM enzyme-specific profiles Link: PRIAM 4.1.2.42
IntEnz Enzyme Link: IntEnz 4.1.2.42
MEDLINE Enzyme Link: MEDLINE 4.1.2.42

EC number:4.1.2.42

MSA:

4.1.2.42;
Phylogenetic Tree:

4.1.2.42;
Uniprot:
M-CSA:
RHEA:20073 D-allothreonine = acetaldehyde + glycine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[CH2;+0:2]-[*:3].[*:5]-[CH;+0:4]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization.Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H1998 Jul 39642221
Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38.Kataoka M, Ikemi M, Morikawa T, Miyoshi T, Nishi K, Wada M, Yamada H, Shimizu S1997 Sep 19346293
Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes.Paiardini A, Contestabile R, D'Aguanno S, Pascarella S, Bossa F2003 Apr 1112686135
Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug.Liu JQ, Odani M, Yasuoka T, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H2000 Jul10952004
A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution.Liu JQ, Odani M, Dairi T, Itoh N, Shimizu S, Yamada H1999 May10390816
RHEA:15257 D-threonine = acetaldehyde + glycine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[CH;+0:4](-[*:5])-[OH;+0:6]>>[*:1]-[CH2;+0:2]-[*:3].[*:5]-[CH;+0:4]=[O;H0;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization.Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H1998 Jul 39642221
Isolation and characterization of D-threonine aldolase, a pyridoxal-5'-phosphate-dependent enzyme from Arthrobacter sp. DK-38.Kataoka M, Ikemi M, Morikawa T, Miyoshi T, Nishi K, Wada M, Yamada H, Shimizu S1997 Sep 19346293
Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes.Paiardini A, Contestabile R, D'Aguanno S, Pascarella S, Bossa F2003 Apr 1112686135
Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug.Liu JQ, Odani M, Yasuoka T, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H2000 Jul10952004
A new route to L-threo-3-[4-(methylthio)phenylserine], a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution.Liu JQ, Odani M, Dairi T, Itoh N, Shimizu S, Yamada H1999 May10390816