Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p)
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Taxol biosynthesis: molecular cloning of a benzoyl-CoA:taxane 2alpha-O-benzoyltransferase cDNA from taxus and functional expression in Escherichia coliMolecular cloning of a 10-deacetylbaccatin III-10-O-acetyl transferase cDNA from Taxus and functional expression in Escherichia coliExpression, purification, and structural analysis of the trimeric form of the catalytic domain of the Escherichia coli dihydrolipoamide succinyltransferaseStructure and Function of the Catalytic Domain of the Dihydrolipoyl Acetyltransferase Component in Escherichia coli Pyruvate Dehydrogenase ComplexMolecular characterization of the salutaridinol 7-O-acetyltransferase involved in morphine biosynthesis in opium poppy Papaver somniferum.Catabolism of branched-chain alpha-keto acids in Enterococcus faecalis: the bkd gene cluster, enzymes, and metabolic route.A synchronized substrate-gating mechanism revealed by cubic-core structure of the bovine branched-chain alpha-ketoacid dehydrogenase complexCloning, overexpression and mutagenesis of cDNA encoding dihydrolipoamide succinyltransferase component of the porcine 2-oxoglutarate dehydrogenase complex.Saccharomyces cerevisiae Atf1p is an alcohol acetyltransferase and a thioesterase in vitro.The E2 domain of OdhA of Corynebacterium glutamicum has succinyltransferase activity dependent on lipoyl residues of the acetyltransferase AceFThe polysialic acid-specific O-acetyltransferase OatC from Neisseria meningitidis serogroup C evolved apart from other bacterial sialate O-acetyltransferases.The terminal O-acetyltransferase involved in vindoline biosynthesis defines a new class of proteins responsible for coenzyme A-dependent acyl transfer.Mutagenesis of conserved active site residues of dihydrolipoamide succinyltransferase enhances the accumulation of α-ketoglutarate in Yarrowia lipolytica.
P2860
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P2860
Crystallographic and enzymatic investigations on the role of Ser558, His610, and Asn614 in the catalytic mechanism of Azotobacter vinelandii dihydrolipoamide acetyltransferase (E2p)
description
1995 nî lūn-bûn
@nan
1995 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@ast
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@en
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@nl
type
label
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@ast
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@en
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@nl
prefLabel
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@ast
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@en
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@nl
P2093
P356
P1433
P1476
Crystallographic and enzymatic ...... oamide acetyltransferase (E2p)
@en
P2093
P304
P356
10.1021/BI00013A018
P407
P577
1995-04-04T00:00:00Z