Sequence of DHE3_BOVIN
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
EC Number:1.4.1.3
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H + H+
Other sequences found for EC No. 1.4.1.3
General information:
Sequence
0 MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLVPPAR RHYSEAAADR
60 EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRETEEQKRN RVRSILRIIK PCNHVLSLSF
120 PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG
180 GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGVD VPAPDMSTGE REMSWIADTY
240 ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
300 DKTFVVQGFG NVGLHSMRYL HRFGAKCITV GESDGSIWNP DGIDPKELED FKLQHGTILG
360 FPKAKIYEGS ILEVDCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER
420 NIMVIPDLYL NAGGVTVSYF EWLNNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK
480 HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV
540 NAIEKVFRVY NEAGVTFT
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
25294
Kim D.W.,Eum W.S.,Jang S.H.,Yoon C.S.,Kim Y.H.,Choi S.H.,Choi H.S.,Kim S.Y.,Kwon H.Y.,Kang J.H.,Kwon O.-S.,Cho S.-W.,Park J.,Choi S.Y.
Molecular gene cloning, expression, and characterization of bovine brain glutamate dehydrogenase.
J. Biochem. Mol. Biol.
36
545-551
2003
25296
Moon K.,Smith E.L.
Sequence of bovine liver glutamate dehydrogenase. 8. Peptides produced by specific chemical cleavages; the complete sequence of the protein.
J. Biol. Chem.
248
3082-3088
1973
25297
Julliard J.H.,Smith E.L.
Partial amino acid sequence of the glutamate dehydrogenase of human liver and a revision of the sequence of the bovine enzyme.
J. Biol. Chem.
254
3427-3438
1979
25298
Witzemann V.,Koberstein R.,Sund H.,Rasched I.,Joernvall H.,Noack K.
Studies of glutamate dehydrogenase: chemical modification and quantitative determination of tryptophan residues.
Eur. J. Biochem.
43
319-325
1974
25299
Rasched I.,Joernvall H.,Sund H.
Studies of glutamate dehydrogenase. Identification of an amino group involved in the substrate binding.
Eur. J. Biochem.
41
603-606
1974
25300
Du J.,Zhou Y.,Su X.,Yu J.J.,Khan S.,Jiang H.,Kim J.,Woo J.,Kim J.H.,Choi B.H.,He B.,Chen W.,Zhang S.,Cerione R.A.,Auwerx J.,Hao Q.,Lin H.
Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase.
Science
334
806-809
2011
25301
Peterson P.E.,Smith T.J.
The structure of bovine glutamate dehydrogenase provides insights into the mechanism of allostery.
Structure
7
769-782
1999
25302
Smith T.J.,Peterson P.E.,Schmidt T.,Fang J.,Stanley C.A.
Structures of bovine glutamate dehydrogenase complexes elucidate the mechanism of purine regulation.
J. Mol. Biol.
307
707-720
2001
25303
Banerjee S.,Schmidt T.,Fang J.,Stanley C.A.,Smith T.J.
Structural studies on ADP activation of mammalian glutamate dehydrogenase and the evolution of regulation.
Biochemistry
42
3446-3456
2003
