Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
about
Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in natureCharacterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triadThe Structure of Allophanate Hydrolase from Granulibacter bethesdensis Provides Insights into Substrate Specificity in the Amidase Signature FamilyPurification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADPIdentification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633.Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth.
P2860
Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
description
2000 nî lūn-bûn
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
2000年论文
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2000年论文
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name
Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
@en
Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
@nl
type
label
Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
@en
Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
@nl
prefLabel
Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
@en
Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
@nl
P2093
P2860
P1433
P1476
Identification of active-site residues in Bradyrhizobium japonicum malonamidase E2.
@en
P2093
P2860
P304
P356
10.1042/0264-6021:3490501
P407
P577
2000-07-01T00:00:00Z