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Literature summary extracted from

  • Goldberg, S.; Goswami, A.; Guo, Z.; Chan, Y.; Lo, E.; Lee, A.; Truc, V.; Natalie, K.; Hang, C.; Rossano, L.; Schmidt, M.
    Preparation of beta-hydroxy-alpha-amino acid using recombinant beta-threonine aldolase (2015), Org. Process Res. Dev., 19, 1308-1316 .
No PubMed abstract available

Application

EC Number Application Comment Organism
4.1.2.42 pharmacology efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization Arthrobacter sp.
4.1.2.42 pharmacology efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization Achromobacter xylosoxidans
4.1.2.42 synthesis efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization Arthrobacter sp.
4.1.2.42 synthesis efficient, environmentally friendly process for the production of (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid by a recombinant D-threonine aldolase catalyzed aldol addition of glycine and pyridine 4-carboxaldehyde. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid, is a key intermediate in the synthesis of the (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-1-(pyrrolidin-1-yl)propan-1-one, a developmental drug candidate. The aldol addition product directly crystallizes out from the reaction mixture in high purity and high diastereo- and enantioselectivity, contributing to high yield and allowing easy isolation, processing, and downstream utilization Achromobacter xylosoxidans

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.2.42 overexpression in Escherichia coli Arthrobacter sp.
4.1.2.42 overexpression in Escherichia coli Achromobacter xylosoxidans

General Stability

EC Number General Stability Organism
4.1.2.42 divalent transition metal cations (cobalt and nickel) improve the stability significantly. Ni2+ is the best and retains almost all activity on storage at 4 °C for a week. Although MnCl2 was required to catalyze the condensation Arthrobacter sp.
4.1.2.42 divalent transition metal cations (cobalt and nickel) improve the stability significantly. Ni2+ is the best and retains almost all activity on storage at 4 °C for a week. Although MnCl2 was required to catalyze the condensation Achromobacter xylosoxidans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.1.2.42 MnCl2 rrequired for condensation reaction Arthrobacter sp.
4.1.2.42 MnCl2 rrequired for condensation reaction Achromobacter xylosoxidans

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.2.42 42000
-
 SDS-PAGE Arthrobacter sp.
4.1.2.42 42000
-
 SDS-PAGE Achromobacter xylosoxidans

Organism

EC Number Organism UniProt Comment Textmining
4.1.2.42 Achromobacter xylosoxidans Q9RBG6
-
-
4.1.2.42 Achromobacter xylosoxidans IFO 12699 Q9RBG6
-
-
4.1.2.42 Arthrobacter sp. O82872
-
-
4.1.2.42 Arthrobacter sp. DK-38 O82872
-
-

Storage Stability

EC Number Storage Stability Organism
4.1.2.42 4°C, enzyme solution prepared by lysing the cells loses about 55% of its initial activity after 1 week of storage Arthrobacter sp.
4.1.2.42 4°C, enzyme solution prepared by lysing the cells loses about 55% of its initial activity after 1 week of storage Achromobacter xylosoxidans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.42 glycine + pyridine-4-carboxaldehyde
-
 Arthrobacter sp. (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
-
 ?
4.1.2.42 glycine + pyridine-4-carboxaldehyde
-
 Achromobacter xylosoxidans (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
-
 ?
4.1.2.42 glycine + pyridine-4-carboxaldehyde
-
 Arthrobacter sp. DK-38 (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
-
 ?
4.1.2.42 glycine + pyridine-4-carboxaldehyde
-
 Achromobacter xylosoxidans IFO 12699 (2R,3S)-2-amino-3-hydroxy-3-(pyridin-4-yl)-propanoic acid
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.2.42 monomer
-
 Arthrobacter sp.
4.1.2.42 monomer
-
 Achromobacter xylosoxidans

Synonyms

EC Number Synonyms Comment Organism
4.1.2.42 ARDTA
-
 Arthrobacter sp.
4.1.2.42 AXDTA
-
 Achromobacter xylosoxidans

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.42 pyridoxal 5'-phosphate rrequired Arthrobacter sp.
4.1.2.42 pyridoxal 5'-phosphate rrequired Achromobacter xylosoxidans