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1 ilization protein (acuC) and acetylpolyamine amidohydrolase.
2 udes pyrazinamidase and N-carbamoylsarcosine amidohydrolase.
3 a larger class of prokaryotic and eukaryotic amidohydrolases.
4 N-terminal nucleophile structural family of amidohydrolases.
5 al mechanism of N-terminal nucleophile (Ntn)-amidohydrolases.
6 vate water for hydrolysis in other class III amidohydrolases.
7 /alpha)(8)-barrel fold characteristic of the amidohydrolases.
8 , and (iii) cleavage under the action of the amidohydrolases.
9 ne (ARGAH1 or ARGAH2 encoding arginine [Arg] amidohydrolase-1 and -2, respectively) resulted in incre
11 thaliana), (1) allantoinase, (2) allantoate amidohydrolase (AAH), (3) ureidoglycine aminohydrolase,
15 ASPS, to the haloacid dehalogenase, enolase, amidohydrolase and crotonase superfamilies and to the se
16 HAEA and 15-HAEA are poor substrates for AEA amidohydrolase and do not bind to the AEA uptake carrier
18 essing of other proteins such as inteins and amidohydrolases, but their mechanisms in such proteins a
20 , the activity of the cobyric acid-producing amidohydrolase CbiZ enzyme is essential for the conversi
21 ay, of archaeal origin, depends on an AdoCbi amidohydrolase (CbiZ) enzyme to generate adenosylcobyric
23 9 is similar to that of N-carbamoylsarcosine amidohydrolase (CSHase) of Arthrobacter sp. and YcaC of
24 The enzyme penicillin acylase (penicillin amidohydrolase EC 3.5.1.11) catalyses the cleavage of th
27 rom five functionally diverse superfamilies (amidohydrolase, enolase, glutathione transferase, haloal
28 salvaging pathway for cobinamide in which an amidohydrolase enzyme cleaves off the aminopropanol moie
29 es the function of a previously unidentified amidohydrolase enzyme that converts adenosylcobinamide t
31 induces the AEA-degrading enzyme fatty acid amidohydrolase (FAAH), and inhibition of FAAH activity p
36 s how the ILR1-like indole acetic acid (IAA) amidohydrolase family of genes has functionally evolved
42 ogy models of a functionally uncharacterized amidohydrolase from Agrobacterium radiobacter K84 (Arad3
43 d sequence identity to TrzD, a cyanuric acid amidohydrolase, from Pseudomonas sp. strain NRRLB-12227.
45 An ortholog for the Arabidopsis IAR3 auxin amidohydrolase gene has been isolated from wheat (TaIAR3
48 agmatine deiminase and N-carbamoylputrescine amidohydrolase in archaea, and of S-adenosylmethionine d
49 docked each metabolite into seven different amidohydrolases in both the ground-state and the high-en
51 terminal Gln by Nt(Q)-amidase, an N-terminal amidohydrolase, is a part of the N-end rule pathway of p
53 mples of enzyme superfamilies, including the amidohydrolase, metallo-beta-lactamase, and enolase supe
54 the sequence of the NTA1-encoded N-terminal amidohydrolase of the yeast Saccharomyces cerevisiae, wh
57 ntains a CHAP (cysteine, histidine-dependent amidohydrolase/peptidase) domain found in bacterial mure
58 d a C-terminal cysteine, histidine-dependent amidohydrolases/peptidases (CHAP) domain in its C-termin
63 residue proposed to activate water in other amidohydrolases, reduced the kcat to a much lesser exten
64 oid anandamide by an inhibitor of fatty acid amidohydrolase reduces blood pressure, cardiac contracti
65 ll fractionation studies showed that the NAE amidohydrolase, responsible for FFA production, was asso
66 nomes sequenced to date, indicating that the amidohydrolase route of ureide degradation is universal
67 extent than what has been reported for other amidohydrolases, suggesting that His-223 has a different
69 e end of beta-strand 8 in all members of the amidohydrolase superfamily abstracts a proton from the m
70 hat AtzB contained the conserved mononuclear amidohydrolase superfamily active-site residues His74, H
73 te hydrolase, EC 3.5.2.7) is a member of the amidohydrolase superfamily and catalyzes the conversion
75 spartyl dipeptidase (IAD) is a member of the amidohydrolase superfamily and catalyzes the hydrolytic
76 possess the signature sequence motifs of the amidohydrolase superfamily and likely share the same str
78 inosa has been identified as a member of the amidohydrolase superfamily by a comprehensive amino acid
80 ce alignment between HutF and members of the amidohydrolase superfamily containing mononuclear metal
87 and Nocardioides spp., is reportedly in the amidohydrolase superfamily of metalloenzymes, but previo
88 is enzyme is a member of the metal-dependent amidohydrolase superfamily of the (beta/alpha)(8) TIM ba
90 etal-ion dependent esterase MGS0169 from the amidohydrolase superfamily revealed a novel active site
92 915 is the second enzyme from cog3618 of the amidohydrolase superfamily that does not require a dival
94 e only documented example of a member in the amidohydrolase superfamily that does not require one or
95 refore the first characterized member in the amidohydrolase superfamily that represents a C-C breakin
96 rogation of uncharacterized enzymes from the amidohydrolase superfamily using a structure-guided appr
98 catalytic activities of three members of the amidohydrolase superfamily were discovered using amino a
99 beta/alpha)(8) barrel and is a member of the amidohydrolase superfamily with a single zinc in the act
100 .0 A confirms that Bh0493 is a member of the amidohydrolase superfamily with conserved residues commo
102 been suggested to consist of members of the amidohydrolase superfamily, a large class of metallohydr
105 ization displays the landmark feature of the amidohydrolase superfamily, showing a metal ligand (iron
106 ructure established that LigY belongs to the amidohydrolase superfamily, unlike previously characteri
107 y further suggests that ACMSD belongs to the amidohydrolase superfamily, whose structurally character
117 ene (termed Ntan1) that encode a 310-residue amidohydrolase (termed NtN-amidase) specific for N-termi
118 ryotic enzyme similar to the acetylpolyamine amidohydrolases that relied on reversible acetylation an
119 have been discovered, including the enolase, amidohydrolase, thiyl radical, crotonase, vicinal-oxygen
120 opanol group of AdoCbi using the CbiZ AdoCbi amidohydrolase to generate adenosylcobyric acid, which i
121 cine aminohydrolase, and (4) ureidoglycolate amidohydrolase (UAH), catalyze the complete hydrolysis o
123 structure of a ternary complex of allantoate amidohydrolase with its substrate allantoate and an allo
124 nic--semialdehyde decarboxylase, a class III amidohydrolase, with a single zinc ion coordinated by Hi
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