Structural relationship between the hexameric and tetrameric family of glutamate dehydrogenases

European Journal of Biochemistry

Volumn 209, Issue 3, 1992, Pages 851-859

  BRITTON, K Linda ^a   BAKER, Patrick J ^a   RICE, David W ^a   STILLMAN, Timothy J ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE DEHYDROGENASE;

ARTICLE; CLOSTRIDIUM; ENZYME STRUCTURE; NEUROSPORA CRASSA; NONHUMAN; PRIORITY JOURNAL; PROTEIN FAMILY;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; CATTLE; CLOSTRIDIUM; GLUTAMATE DEHYDROGENASE; GLUTAMATES; GLUTAMIC ACID; MOLECULAR SEQUENCE DATA; NEUROSPORA CRASSA; NUCLEOTIDES; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; SUPPORT, NON-U.S. GOV'T;

CLOSTRIDIUM SYMBIOSUM; NEUROSPORA CRASSA;

EID: 0026463143     PISSN: 00142956     EISSN: 14321033     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1992.tb17357.x     Document Type: Article

References (42)

1. L-Glutamate Dehydrogenases* *Research work cited in this review which originates in the author's laboratory was supported in part by research grant AM 13332, United States Public Health Service and research grant GB 26583X from the National Science Foundation.
2. Identification of three essential lysine residues probably involved in substrate binding of the NAD+- dependent glutamate dehydrogenase ofClostridium symbiosum
3. L-glutamic acid dehydrogenase; structural requirements for substrate competition; effect of thyroxine.
4. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures