Clarifying the catalytic roles of conserved residues in the amidase signature family.
about
Structure of malonamidase E2 reveals a novel Ser-cisSer-Lys catalytic triad in a new serine hydrolase fold that is prevalent in natureIdentification of a novel amidase motif in neutral ceramidaseThe nitrilase superfamily: classification, structure and functionCharacterization of a novel Ser-cisSer-Lys catalytic triad in comparison with the classical Ser-His-Asp triadBinding and Inactivation Mechanism of a Humanized Fatty Acid Amide Hydrolase by α-Ketoheterocycle Inhibitors Revealed from Cocrystal StructuresX-ray Crystallographic Analysis of α-Ketoheterocycle Inhibitors Bound to a Humanized Variant of Fatty Acid Amide HydrolaseFluoride-Mediated Capture of a Noncovalent Bound State of a Reversible Covalent Enzyme Inhibitor: X-ray Crystallographic Analysis of an Exceptionally Potent α-Ketoheterocycle Inhibitor of Fatty Acid Amide HydrolaseReversible Competitive α-Ketoheterocycle Inhibitors of Fatty Acid Amide Hydrolase Containing Additional Conformational Constraints in the Acyl Side Chain: Orally Active, Long-Acting AnalgesicsRational Design of Fatty Acid Amide Hydrolase Inhibitors That Act by Covalently Bonding to Two Active Site ResiduesCrystal structure of the dopamine N -acetyltransferase–acetyl-CoA complex provides insights into the catalytic mechanismFatty acid amide hydrolase as a potential therapeutic target for the treatment of pain and CNS disordersUnconventional serine proteases: variations on the catalytic Ser/His/Asp triad configurationComplete nucleotide sequence and organization of the atrazine catabolic plasmid pADP-1 from Pseudomonas sp. strain ADPEffects of pH on the inhibition of fatty acid amidohydrolase by ibuprofenEnzymatic pathways that regulate endocannabinoid signaling in the nervous systemEvidence for distinct roles in catalysis for residues of the serine-serine-lysine catalytic triad of fatty acid amide hydrolasePurification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADPα-Ketoheterocycle inhibitors of fatty acid amide hydrolase: exploration of conformational constraints in the acyl side chain.The discovery and development of inhibitors of fatty acid amide hydrolase (FAAH).Cannabinoid receptors are absent in insects.Identification and recombinant expression of anandamide hydrolyzing enzyme from Dictyostelium discoideum.Aliphatic and enantioselective amidases: from hydrolysis to acyl transfer activity.Identification and characterization of a mandelamide hydrolase and an NAD(P)+-dependent benzaldehyde dehydrogenase from Pseudomonas putida ATCC 12633.α-Ketoheterocycle-based Inhibitors of Fatty Acid Amide Hydrolase (FAAH).Discovery of a potent, selective, and efficacious class of reversible alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase effective as analgesicsPotent and selective alpha-ketoheterocycle-based inhibitors of the anandamide and oleamide catabolizing enzyme, fatty acid amide hydrolaseStructure-activity relationships of alpha-ketooxazole inhibitors of fatty acid amide hydrolaseOptimization of the central heterocycle of alpha-ketoheterocycle inhibitors of fatty acid amide hydrolase.Exploration of a fundamental substituent effect of alpha-ketoheterocycle enzyme inhibitors: Potent and selective inhibitors of fatty acid amide hydrolase.Optimization of alpha-ketooxazole inhibitors of fatty acid amide hydrolase.Design, synthesis, and characterization of α-ketoheterocycles that additionally target the cytosolic port Cys269 of fatty acid amide hydrolaseFunctional characterization of cis-elements conferring vascular vein expression of At4g34880 amidase family protein gene in ArabidopsisHydrazidase, a novel amidase signature enzyme that hydrolyzes acylhydrazides.Mutations in Arabidopsis fatty acid amide hydrolase reveal that catalytic activity influences growth but not sensitivity to abscisic acid or pathogens.pH-, temperature- and ion-dependent oligomerization of Sulfolobus solfataricus recombinant amidase: a study with site-specific mutantsPurification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth.Oligomerization of Sulfolobus solfataricus signature amidase is promoted by acidic pH and high temperature.Quantum mechanics/molecular mechanics modeling of fatty acid amide hydrolase reactivation distinguishes substrate from irreversible covalent inhibitors.Gene expression in insecticide resistant and susceptible Anopheles gambiae strains constitutively or after insecticide exposure.Molecular identification of a functional homologue of the mammalian fatty acid amide hydrolase in Arabidopsis thaliana.
P2860
Q24536561-95C71851-2CEA-4E88-A1A0-F43AED0C5A0AQ24537468-D6D0F351-BBB6-4539-9262-0E5DA78F12F5Q24551006-828E8D1B-0560-4216-86A1-63FB6B514567Q27641048-7AFF7392-C4B1-4BAE-A778-2A26BF4A35E4Q27657268-7E424083-485C-447B-8783-2A43E3D071F5Q27658264-2C131907-0DC6-4365-9AE6-029EA3DB9412Q27667078-B18A7690-6CBE-4D6C-927A-3938FA83C833Q27667312-B0283C08-6BF0-4649-9961-7BF6ED00BD00Q27677344-4562CFC0-7545-441C-9084-51C8A4971CC4Q27681264-EA3AC825-4C05-496E-B361-DA00DDE2F3E9Q28285103-6AB07E58-483C-4BAE-950D-AB447B47756DQ28295493-7FBC98AB-722E-4DBB-8866-A67E07517C3AQ28349622-86BFAB15-3C6F-47FB-82C9-B8DCCF2E5329Q28366569-2587A263-6469-4762-9FA3-060306A434D5Q28390932-8B112741-5DFC-4339-9E21-D3AB25ADC4C6Q28570492-B9F31D60-50E8-40ED-92D5-61AD30404346Q33215304-96BFFF30-94CD-4F17-A933-D560B222C3CEQ33644120-CCF25310-A6F0-40FB-93FC-129FE66F7F72Q34027721-1366E520-1FD9-413D-9D24-FF87F5D7DC12Q34083619-D1455604-50CB-439C-9112-14271425E93AQ34316389-8180FC0C-A927-4A30-A39E-C784AEAB35E4Q34369647-0A97A3CC-F8B8-4932-9C81-8565884418B2Q34891664-AC3A95F3-D60E-4D00-872A-BF65C8EC9778Q35986269-A7B1246B-2BD0-4707-B708-6CD9B52DA7BDQ36803312-BB77B8EF-D9EC-4493-A044-DABF23B7D722Q36865744-7FEAA32C-CBBD-480D-A992-8486C1CB37F5Q36865750-AEF4A63C-AEAC-4514-94F4-47CC03C76B17Q36914902-AC53BE69-CF2B-4277-88B1-BEE0A1D70402Q36970033-84724BDE-4B8E-4595-815D-6A47FC4FDBFEQ37325801-7A13EC27-B1AA-4FBB-A092-252509FF86C2Q37613654-B1F127C4-D56B-4E02-99F2-72C433211BAEQ41288889-6925CECC-6EC9-4C63-A87C-D799BF7BCD8DQ41589584-7AE950CF-C114-412A-8C33-03DCE60DE553Q41856734-DA409801-FB14-490C-88FF-9C6F6182B5F0Q42134004-A2FCE7AF-A064-4150-B1CE-C13BB57B916AQ42240705-928C3AD0-BFAC-4DAE-A06A-5BEF0DD4CB04Q42871151-87B01750-FA52-4EEB-BB32-102F31F9667FQ43072779-8F5C8EBD-2370-4397-9C14-CDA1D23FFEC9Q44165965-D7A48C86-BA1A-4018-8C9C-83F683465B8FQ44489713-5A2E5D0E-7F56-45B1-A27E-B3AD2AA983FE
P2860
Clarifying the catalytic roles of conserved residues in the amidase signature family.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
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
@zh
2000年论文
@zh-cn
name
Clarifying the catalytic roles of conserved residues in the amidase signature family.
@en
type
label
Clarifying the catalytic roles of conserved residues in the amidase signature family.
@en
prefLabel
Clarifying the catalytic roles of conserved residues in the amidase signature family.
@en
P2860
P356
P1476
Clarifying the catalytic roles of conserved residues in the amidase signature family.
@en
P2093
B F Cravatt
M P Patricelli
P2860
P304
19177-19184
P356
10.1074/JBC.M001607200
P407
P577
2000-06-01T00:00:00Z