-
Transaminases or
aminotransferases are
enzymes that
catalyze a
transamination reaction between an
amino acid and an α-keto acid. They are
important in...
- "Escherichia coli
mutants deficient in the
aspartate and
aromatic amino acid
aminotransferases".
Journal of Bacteriology. 130 (1): 429–440. doi:10.1128/JB.130.1...
- L-alanine + α-ketoglutarate ⇌
pyruvate + L-glutamate ALT (and all
aminotransferases)
require the
coenzyme pyridoxal phosphate,
which is
converted into...
- 372 residues. The
biological function of branched-chain
amino acid
aminotransferases is to
catalyse the
synthesis or
degradation of the
branched chain...
- leucine. The two
common types of
aminotransferases are
alanine aminotransferase (ALT) and
aspartate aminotransferase (AST). Booth,
Gerald (2000-01-01)...
- transferases, and
other enzymes including cysteine desulphurase EC:4.4.1.-.
Aminotransferases share certain mechanistic features with
other pyridoxal- phosphate...
-
blood levels of
enzymes found primarily from the liver, such as the
aminotransferases (ALT, AST), and
alkaline phosphatase (ALP);
bilirubin (which causes...
-
phosphoserine aminotransferase, 3-phosphoserine
aminotransferase,
hydroxypyruvic phosphate-glutamic transaminase, L-phosphoserine
aminotransferase, phosphohydroxypyruvate...
-
using X-ray
crystallography and
shows similarity to
other subgroup 2
aminotransferases such as
dialkyglucine decarboxylatse. The OAT
protein functions as...
-
Matringe M (2014). "Three
different classes of
aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms"...
