Reference on EC 2.6.1.21 - D-amino-acid transaminase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martinez-Carrion, M.; Jenkins, W.T.
D-Alanine-D-glutamate transaminase. I. Purification and characterization
J. Biol. Chem.
240
3538-3546
1965
Bacillus subtilis
Martinez-Carrion, M.; Jenkins, W.T.
D-Alanine-D-glutamate transaminase. II. Inhibitors and the mechanism of transamination of D-amino acids
J. Biol. Chem.
240
3547-3552
1965
Bacillus subtilis
Ogawa, T.; Fukuda, M.
Occurrence of D-amino acid aminotransferase in pea seedlings
Biochem. Biophys. Res. Commun.
52
998-1002
1973
Pisum sativum
Soper, T.S.; Jones, W.M.; Lerner, B.; Trop, M.; Manning, J.M.
Inactivation of bacterial D-amino acid transaminase by beta-chloro-D-alanine
J. Biol. Chem.
252
3170-3175
1977
Lysinibacillus sphaericus
Soper, T.S.; Manning, J.M.; Marcotte, P.A.; Walsh, C.T.
Inactivation of bacterial D-amino acid transaminases by the olefinic amino acid D-vinylglycine
J. Biol. Chem.
252
1571-1575
1977
Bacillus subtilis, Lysinibacillus sphaericus
Gosling, J.P.; Fottrell, P.F.
The partial purification and some properties of D-alanine aminotransferase from Rhizobium japonicum
Biochem. Soc. Trans.
1
252-254
1973
Bradyrhizobium japonicum
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Yonaha, K.; Misono, H.; Yamamoto, T.; Soda, K.
D-amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties
J. Biol. Chem.
250
6983-6989
1975
Lysinibacillus sphaericus
Kishimoto, K.; Yoshimura, T.; Esaki, N.; Sugio, S.; Manning, J.M.; Soda, K.
Role of leucine 201 of thermostable D-amino acid aminotransferase from a thermophile, Bacillus sp. YM-1
J. Biochem.
117
691-696
1995
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) YM-1
Sugio, S.; Petsko, G.A.; Manning, J.M.; Soda, K.; Ringe, D.
Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity
Biochemistry
34
9661-9669
1995
Bacillus sp. (in: Bacteria), Lysinibacillus sphaericus
Ro, H.S.; Hong, S.P.; Seo, H.J.; Yoshimura, T.; Esaki, N.; Soda, K.; Kim, H.S.; Sung, M.H.
Site-directed mutagenesis of the amino acid residues in beta-strand III [Val30-Val36] of D-amino acid aminotransferase of Bacillus sp. YM-1
FEBS Lett.
398
141-145
1996
Bacillus sp. (in: Bacteria)
Fuchikami, Y.; Yoshimura, T.; Gutierrez, A.; Soda, K.; Esaki, N.
Construction and properties of a fragmentary D-amino acid aminotransferase
J. Biochem.
124
905-910
1998
Bacillus sp. (in: Bacteria)
Gutierrez, A.; Yoshimura, T.; Fuchikami, Y.; Soda, K.; Esaki, N.
A mutant D-amino acid aminotransferase with broad substrate specificity: construction by replacement of the interdomain loop Pro119-Arg120-Pro121 by Gly-Gly-Gly
Protein Eng.
11
53-58
1998
Bacillus sp. (in: Bacteria)
Sugio, S.; Kashima, A.; Kishimoto, K.; Peisach, D.; Petsko, G.A.; Ringe, D.; Yoshimura, T.; Esaki, N.
Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination
Protein Eng.
11
613-619
1998
Bacillus sp. (in: Bacteria)
Peisach, D.; Chipman, D.M.; Van Ophem, P.W.; Manning, J.M.; Ringe, D.
Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase
Biochemistry
37
4958-4967
1998
Bacillus sp. (in: Bacteria) (P19938), Bacillus sp. (in: Bacteria)
Gutierrez, A.; Yoshimura, T.; Fuchikami, Y.; Esaki, N.
Modulation of activity and substrate specificity by modifying the backbone length of the distant interdomain loop of D-amino acid aminotransferase
Eur. J. Biochem.
267
7218-7223
2000
Bacillus sp. (in: Bacteria)
Ro, H.S.
Effects of salts on the conformation and catalytic properties of D-amino acid aminotransferase
J. Biochem. Mol. Biol.
35
306-312
2002
Bacillus sp. (in: Bacteria)
Schtzle, S.; Steffen-Munsberg, F.; Thontowi, A.; Hhne, M.; Robins, K.; Bornscheuer, U.
Enzymatic asymmetric synthesis of enantiomerically pure aliphatic, aromatic and arylaliphatic amines with (R)-selective amine transaminases
Adv. Synth. Catal.
353
2439-2445
2011
Aspergillus fischeri, Aspergillus fumigatus, Aspergillus oryzae, Aspergillus terreus, Fusarium graminearum, Penicillium chrysogenum, Mycolicibacterium vanbaalenii
-
Du, Y.; Dong, W.; Jiang, J.; Chen, Q.; Feng, J.; Wu, Q.; Zhu, D.
[Expression and characterization of a novel ?-transaminase from Burkholderia phytofirmans PsJN].
Sheng Wu Gong Cheng Xue Bao
32
912-926
2016
Paraburkholderia phytofirmans, Paraburkholderia phytofirmans PsJN
Mortuza, R.; Aung, H.L.; Taiaroa, G.; Opel-Reading, H.K.; Kleffmann, T.; Cook, G.M.; Krause, K.L.
Overexpression of a newly identified D-amino acid transaminase in Mycobacterium smegmatis complements glutamate racemase deletion
Mol. Microbiol.
107
198-213
2018
Mycolicibacterium smegmatis (A0R4D5), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc2155 (A0R4D5)
Voss, M.; Xiang, C.; Esque, J.; Nobili, A.; Menke, M.J.; Andre, I.; Hoehne, M.; Bornscheuer, U.T.
Creation of (R)-amine transaminase activity within an alpha-amino acid transaminase scaffold
ACS Chem. Biol.
15
416-424
2020
Bacillus sp. (in: Bacteria) (P19938), Bacillus sp. (in: Bacteria) YM-1 (P19938)
Yu, Y.; Yang, J.; Zheng, L.; Sheng, Q.; Li, C.; Wang, M.; Zhang, X.; McMinn, A.; Zhang, Y.; Song, X.; Chen, X.
Diversity of D-amino acid utilizing bacteria from Kongsfjorden, Arctic, and the metabolic pathways for seven D-amino acids
Front. Microbiol.
10
2983
2020
Halomonas titanicae (A0A558JDR6), Halomonas titanicae SM1922 (A0A558JDR6)
Suarez, J.; Hener, C.; Lehnhardt, V.A.; Hummel, S.; Stahl, M.; Kolukisaoglu, U.e.
AtDAT1 is a key enzyme of D-amino acid stimulated ethylene production in Arabidopsis thaliana
Front. Plant Sci.
10
1609
2019
Arabidopsis thaliana (Q8L493), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q8L493)
Khrenova, M.; Zavyalova, S.; Bezsudnova, E.
Molecular mechanism of stereospecificity toward D-leucine of the transaminase from Desulfohalobium retbaense revealed by molecular dynamic simulations
Moscow Univ. Chem. Bull.
75
167-171
2020
Desulfohalobium retbaense (C8X272), Desulfohalobium retbaense ATCC 49708 (C8X272), Desulfohalobium retbaense DSM 5692 (C8X272), Desulfohalobium retbaense HR100 (C8X272), Desulfohalobium retbaense JCM 16813 (C8X272)
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