Sequence of DHE2_CLOSY
EC Number:1.4.1.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-glutamate + H2O + NAD+ = 2-oxoglutarate + NH3 + NADH + H+
Other sequences found for EC No. 1.4.1.2
General information:
Sequence
0 MSKYVDRVIA EVEKKYADEP EFVQTVEEVL SSLGPVVDAH PEYEEVALLE RMVIPERVIE
60 FRVPWEDDNG KVHVNTGYRV QFNGAIGPYK GGLRFAPSVN LSIMKFLGFE QAFKDSLTTL
120 PMGGAKGGSD FDPNGKSDRE VMRFCQAFMT ELYRHIGPDI DVPAGDLGVG AREIGYMYGQ
180 YRKIVGGFYN GVLTGKARSF GGSLVRPEAT GYGSVYYVEA VMKHENDTLV GKTVALAGFG
240 NVAWGAAKKL AELGAKAVTL SGPDGYIYDP EGITTEEKIN YMLEMRASGR NKVQDYADKF
300 GVQFFPGEKP WGQKVDIIMP CATQNDVDLE QAKKIVANNV KYYIEVANMP TTNEALRFLM
360 QQPNMVVAPS KAVNAGGVLV SGFEMSQNSE RLSWTAEEVD SKLHQVMTDI HDGSAAAAER
420 YGLGYNLVAG ANIVGFQKIA DAMMAQGIAW
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
284291
Teller J.K.,Smith R.M.,McPherson M.J.,Engel P.C.,Guest J.R.
The glutamate dehydrogenase gene of Clostridium symbiosum. Cloning by polymerase chain reaction, sequence analysis and over-expression in Escherichia coli.
Eur. J. Biochem.
206
151-159
1992
284292
Lilley K.S.,Baker P.J.,Britton K.L.,Stillman T.J.,Brown P.E.,Moir A.J.G.,Engel P.C.,Rice D.W.,Bell J.E.,Bell E.
The partial amino acid sequence of the NAD(+)-dependent glutamate dehydrogenase of Clostridium symbiosum: implications for the evolution and structural basis of coenzyme specificity.
Biochim. Biophys. Acta
1080
191-197
1991
284293
Lilley K.S.,Engel P.C.
The essential active-site lysines of clostridial glutamate dehydrogenase. A study with pyridoxal-5'-phosphate.
Eur. J. Biochem.
207
533-540
1992
284294
Dean J.L.,Wang X.G.,Teller J.K.,Waugh M.L.,Britton K.L.,Baker P.J.,Stillman T.J.,Martin S.R.,Rice D.W.,Engel P.C.
The catalytic role of aspartate in the active site of glutamate dehydrogenase.
Biochem. J.
301
13-16
1994
284295
Syed S.E.,Hornby D.P.,Brown P.E.,Fitton J.E.,Engel P.C.
Site and significance of chemically modifiable cysteine residues in glutamate dehydrogenase of Clostridium symbiosum and the use of protection studies to measure coenzyme binding.
Biochem. J.
298
107-113
1994
284296
Baker P.J.,Britton K.L.,Engel P.C.,Farrants G.W.,Lilley K.S.,Rice D.W.,Stillman T.J.
Subunit assembly and active site location in the structure of glutamate dehydrogenase.
Proteins
12
75-86
1992
284297
Stillman T.J.,Baker P.J.,Britton K.L.,Rice D.W.
Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis.
J. Mol. Biol.
234
1131-1139
1993
284298
Yip K.S.P.,Stillman T.J.,Britton K.L.,Artymiuk P.J.,Baker P.J.,Sedelnikova S.E.,Engel P.C.,Pasquo A.,Chiaraluce R.,Consalvi V.,Scandurra R.,Rice D.W.
The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures.
Structure
3
1147-1158
1995
284299
Baker P.J.,Waugh M.L.,Wang X.G.,Stillman T.J.,Turnbull A.P.,Engel P.C.,Rice D.W.
Determinants of substrate specificity in the superfamily of amino acid dehydrogenases.
Biochemistry
36
16109-16115
1997
284300
Stillman T.J.,Migueis A.M.,Wang X.G.,Baker P.J.,Britton K.L.,Engel P.C.,Rice D.W.
Insights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum.
J. Mol. Biol.
285
875-885
1999
