TY - JOUR
T1 - A new family of 2-hydroxyacid dehydrogenases
AU - Grant, Gregory A.
N1 - Funding Information:
Sequence relatedness was determined with the ALIGN program of the Protein National Biomedical Research Foundation. This program uses a version of the (3) algorithm with the mutation data matrix which generates an alignment score indication of relatedness.
PY - 1989/12/30
Y1 - 1989/12/30
N2 - The NADH-dependent hydroxypyruvate reductase from cucumber and the pdxB gene product of E. coli display significant homology to E. coli D-3-phosphoglycerate dehydrogenase. In contrast, these proteins do not display much similarity with other oxidoreductases or with other 2-hydroxyacid dehydrogenases in particular. On the basis of their relatedness and the structure of their substrates, these three enzymes constitute a new family of 2-hydroxyacid dehydrogenases distinct from malate and lactate dehydrogenase.
AB - The NADH-dependent hydroxypyruvate reductase from cucumber and the pdxB gene product of E. coli display significant homology to E. coli D-3-phosphoglycerate dehydrogenase. In contrast, these proteins do not display much similarity with other oxidoreductases or with other 2-hydroxyacid dehydrogenases in particular. On the basis of their relatedness and the structure of their substrates, these three enzymes constitute a new family of 2-hydroxyacid dehydrogenases distinct from malate and lactate dehydrogenase.
UR - http://www.scopus.com/inward/record.url?scp=0024835757&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(89)92755-1
DO - 10.1016/0006-291X(89)92755-1
M3 - Article
C2 - 2692566
AN - SCOPUS:0024835757
SN - 0006-291X
VL - 165
SP - 1371
EP - 1374
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -