Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
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Enzyme
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Query: UNIPROT:Q07644 (
polypeptide
)
72,197
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The regulation of Fd-glutamate synthase (Fd-GOGAT,
EC 1.4.1.7
) and NADH-glutamate synthase (NADH-GOGAT, EC 1.4.1.14) was investigated in maize (Zea mays L. cv. DEA) (1) during development starting from 7- to 11-day-old seedlings, (2) by treatment of 7-day-old etiolated leaves with intermittent light pulses to activate (red) and inactivate (far-red) phytochromes and (3) in 7-day-old green leaves grown under 16-h light/8-h dark cycles. Fd-GOGAT mRNA accumulated 4-fold, and the enzyme
polypeptide
(3-fold) and activity (3-fold) also increased in leaf cells, while NADH-GOGAT activity remained constantly low. Leaf-specific induction of Fd-GOGAT mRNA (3-fold) occurred in etiolated leaves by low fluence red light, and far-red light reversibly repressed the mRNA accumulation. Red/far-red reversible induction also occurred for Fd-GOGAT
polypeptide
(2-fold) and activity (2-fold), implicating the phytochrome-dependent induction of Fd-GOGAT. In contrast, NADH-GOGAT activity remained constant, irrespective of red/far-red light treatments. Fd-GOGAT showed diurnal changes under light/dark cycles with the maximum early in the morning and the minimum in the afternoon at the levels of mRNA, enzyme
polypeptide
and activity. Gln diurnally changed in parallel with Fd-GOGAT mRNA. The induction of Fd-GOGAT provides evidence that light and metabolites are the major signal for the Gln and Glu formation in maize leaf cells.
...
PMID:Regulation by light and metabolites of ferredoxin-dependent glutamate synthase in maize. 1147 12
The structural gene for NADP+-dependent
serine dehydrogenase
[EC 1.1.1.-] from Agrobacterium tumefaciens ICR 1600 was cloned into Escherichia coli cells and its complete DNA sequence was analyzed. The gene encodes a
polypeptide
containing 249 amino acid residues. The enzyme had high sequence similarity to short-chain alcohol dehydrogenases from bacteria and unknown proteins of Haemophilus influenzae, Escherichia coli, and Saccharomyces cerevisiae.
...
PMID:Cloning and sequencing of the serine dehydrogenase gene from Agrobacterium tumefaciens. 1209 31