Reference on EC 4.2.1.113 - o-succinylbenzoate synthase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thompson, T.B.; Garrett, J.B.; Taylor, E.A.; Meganathan, R.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activity in the enolase superfamily: structure of o-succinylbenzoate synthase from Escherichia coli in complex with Mg2+ and o-succinylbenzoate
Biochemistry
39
10662-10676
2000
Escherichia coli (P29208), Escherichia coli
Klenchin, V.A.; Taylor Ringia, E.A.; Gerlt, J.A.; Rayment, I.
Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate synthase from Escherichia coli
Biochemistry
42
14427-14433
2003
Escherichia coli (P29208), Escherichia coli
Weische, A.; Garvert, W.; Leistner, E.
Biosynthesis of o-succinylbenzoic acid. II.: Properties of o-succinylbenzoic acid synthase, an enzyme involved in vitamin K2 biosynthesis
Arch. Biochem. Biophys.
256
223-231
1987
Escherichia coli, Escherichia coli AN 154
Taylor Ringia, E.A.; Garrett, J.B.; Thoden, J.B.; Holden, H.M.; Rayment, I.; Gerlt, J.A.
Evolution of enzymatic activity in the enolase superfamily: functional studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis
Biochemistry
43
224-229
2004
Amycolatopsis sp.
Thoden, J.B.; Taylor Ringia, E.A.; Garrett, J.B.; Gerlt, J.A.; Holden, H.M.; Rayment, I.
Evolution of enzymatic activity in the enolase superfamily: structural studies of the promiscuous o-succinylbenzoate synthase from Amycolatopsis
Biochemistry
43
5716-5727
2004
Amycolatopsis sp., Amycolatopsis sp. T-1-60
Glasner, M.E.; Fayazmanesh, N.; Chiang, R.A.; Sakai, A.; Jacobson, M.P.; Gerlt, J.A.; Babbitt, P.C.
Evolution of structure and function in the o-succinylbenzoate synthase/N-acylamino acid racemase family of the enolase superfamily
J. Mol. Biol.
360
228-250
2006
Amycolatopsis sp.
Pulaganti, M.; Banaganapalli, B.; Mulakayala, C.; Chitta, S.K.; C M, A.
Molecular modeling and docking studies of O-succinylbenzoate synthase of M. tuberculosis - a potential target for antituberculosis drug design
Appl. Biochem. Biotechnol.
172
1407-1432
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
Brizendine, A.M.; Odokonyero, D.; McMillan, A.W.; Zhu, M.; Hull, K.; Romo, D.; Glasner, M.E.
Promiscuity of Exiguobacterium sp. AT1b o-succinylbenzoate synthase illustrates evolutionary transitions in the OSBS family
Biochem. Biophys. Res. Commun.
450
679-684
2014
Exiguobacterium sp., Exiguobacterium sp. AT1b
Zhu, W.W.; Wang, C.; Jipp, J.; Ferguson, L.; Lucas, S.N.; Hicks, M.A.; Glasner, M.E.
Residues required for activity in Escherichia coli o-succinylbenzoate synthase (OSBS) are not conserved in all OSBS enzymes
Biochemistry
51
6171-6181
2012
Escherichia coli
Odokonyero, D.; Ragumani, S.; Lopez, M.S.; Bonanno, J.B.; Ozerova, N.D.; Woodard, D.R.; Machala, B.W.; Swaminathan, S.; Burley, S.K.; Almo, S.C.; Glasner, M.E.
Divergent evolution of ligand binding in the o-succinylbenzoate synthase family
Biochemistry
52
7512-7521
2013
Escherichia coli (P29208), Escherichia coli, Thermobifida fusca (Q47Q21), Thermobifida fusca
Pulaganti, M.; Banaganapalli, B.; Mulakayala, C.; Chitta, S.; Anuradha, C.
Molecular modeling and docking studies of O-succinylbenzoate synthase of M. tuberculosis - a potential target for antituberculosis drug design
Appl. Biochem. Biotechnol.
172
1407-1432
2014
Mycobacterium tuberculosis (P9WJP3), Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618 / H37Rv (P9WJP3)
Odokonyero, D.; McMillan, A.W.; Ramagopal, U.A.; Toro, R.; Truong, D.P.; Zhu, M.; Lopez, M.S.; Somiari, B.; Herman, M.; Aziz, A.; Bonanno, J.B.; Hull, K.G.; Burley, S.K.; Romo, D.; Almo, S.C.; Glasner, M.E.
Comparison of Alicyclobacillus acidocaldarius o-succinylbenzoate synthase to its promiscuous N-succinylamino acid racemase/o-succinylbenzoate synthase relatives
Biochemistry
57
3676-3689
2018
Alicyclobacillus acidocaldarius subsp. acidocaldarius (C8WS29), Alicyclobacillus acidocaldarius subsp. acidocaldarius ATCC 27009 / DSM 446 / JCM 5260 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-1A (C8WS29)
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