An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates.
about
Biochemical and structural exploration of the catalytic capacity of Sulfolobus KDG aldolasesCrystal structure and stereochemical studies of KD(P)G aldolase from Thermoproteus tenaxStructural Basis for Substrate Specificity and Mechanism of N -Acetyl- d -neuraminic Acid Lyase from Pasteurella multocidaStructural basis of thermal stability of the tungsten cofactor synthesis protein MoaB from Pyrococcus furiosusHyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostabilityCharacterization of a novel N-acetylneuraminic acid lyase favoring N-acetylneuraminic acid synthesisReconstruction of the central carbohydrate metabolism of Thermoproteus tenax by use of genomic and biochemical dataA new intrinsic thermal parameter for enzymes reveals true temperature optima.Identification and characterization of Thermoplasma acidophilum glyceraldehyde dehydrogenase: a new class of NADP+-specific aldehyde dehydrogenase.Improving low-temperature activity of Sulfolobus acidocaldarius 2-keto-3-deoxygluconate aldolase."Hot standards" for the thermoacidophilic archaeon Sulfolobus solfataricus.Bioconversion of D-galacturonate to keto-deoxy-L-galactonate (3-deoxy-L-threo-hex-2-ulosonate) using filamentous fungiThe semi-phosphorylative Entner-Doudoroff pathway in hyperthermophilic archaea: a re-evaluation.Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.The unique features of glycolytic pathways in Archaea.A Novel Aldo-Keto Reductase, HdRed, from the Pacific Abalone Haliotis discus hannai, Which Reduces Alginate-derived 4-Deoxy-L-erythro-5-hexoseulose Uronic Acid to 2-Keto-3-deoxy-D-gluconate.Biochemical characterization of prephenate dehydrogenase from the hyperthermophilic bacterium Aquifex aeolicusCloning, expression, purification, crystallization and preliminary X-ray diffraction studies of N-acetylneuraminate lyase from methicillin-resistant Staphylococcus aureus.The introduction of the fungal D-galacturonate pathway enables the consumption of D-galacturonic acid by Saccharomyces cerevisiae.Systems biology of the modified branched Entner-Doudoroff pathway in Sulfolobus solfataricus.Metabolic pathway of 3,6-anhydro-D-galactose in carrageenan-degrading microorganisms.Cell fusion and hybrids in Archaea: prospects for genome shuffling and accelerated strain development for biotechnology.Metabolism of pentose sugars in the hyperthermophilic archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius.Characterization of a novel Agrobacterium tumefaciens galactarolactone cycloisomerase enzyme for direct conversion of D-galactarolactone to 3-deoxy-2-keto-L-threo-hexarate.Establishment of oxidative D-xylose metabolism in Pseudomonas putida S12.Key Enzymes of the Semiphosphorylative Entner-Doudoroff Pathway in the Haloarchaeon Haloferax volcanii: Characterization of Glucose Dehydrogenase, Gluconate Dehydratase, and 2-Keto-3-Deoxy-6-Phosphogluconate Aldolase.Gluconate dehydratase from the promiscuous Entner-Doudoroff pathway in Sulfolobus solfataricus.Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase.Carrageenan catabolism is encoded by a complex regulon in marine heterotrophic bacteria.Macromolecular rate theory (MMRT) provides a thermodynamics rationale to underpin the convergent temperature response in plant leaf respiration.A systems biology approach reveals major metabolic changes in the thermoacidophilic archaeon Sulfolobus solfataricus in response to the carbon source L-fucose versus D-glucose.Sulfolobus - A Potential Key Organism in Future Biotechnology.Sulfolobus acidocaldarius uptakes pentoses via a cut2-type ABC transporter and metabolizes them through the aldolase-independent Weimberg pathway.Identification of a dimeric KDG aldolase from Agrobacterium tumefaciens.Production of ethylene glycol or glycolic acid from D-xylose in Saccharomyces cerevisiae.The crystal structure of D-xylonate dehydratase reveals functional features of enzymes from the Ilv/ED dehydratase family.Exploring D-xylose oxidation in Saccharomyces cerevisiae through the Weimberg pathway.Dynamical origins of heat capacity changes in enzyme-catalysed reactions.
P2860
Q27640837-96CC8457-E3D9-45B5-A299-816D967C1038Q27649511-B54906CB-E134-41F4-9BD3-B295FCBD5ECCQ27680435-4635B6BC-2157-4BF7-A625-494896FB7D0DQ27681467-F0057085-3021-4E09-8B68-72223B6BDBCEQ28203641-1CE56B1A-8B3E-42FE-B217-0A88AFD65480Q28854128-AAC59B0E-4D74-4834-9426-BF298C07E165Q30913745-3D957476-9B35-4930-A7AB-6776B9C736A6Q33198416-2A1B1B29-A91A-483F-9473-2148EC86A2AFQ33237746-58F72543-A22C-4C39-941D-342576D9090CQ33455570-7867BD47-269B-46ED-8E6B-C247A6312E92Q33554345-B036CD3A-B157-4F01-B3FA-6E6C5330215EQ33675418-74247E90-85F1-420D-9013-5AFEB77405E3Q33986860-B191819A-9586-43F1-9884-D54AD439D9CFQ34408562-09807BB3-6830-480E-8886-E5CB34EBE90EQ35201066-B0C457E2-EBF6-4E37-970B-DB6865131DF9Q36407279-441F8079-A0E0-4598-A8A6-926FF348CB9EQ36491031-ED4427B4-0B5B-4936-832C-994B78458708Q36711083-227A08BA-04FE-4440-8B95-BD2F617CBB77Q37188796-0970BC08-0226-4D0E-B474-9232DF7ECBF5Q38686300-CCE5ED6F-F369-4EEB-A379-F186A554502DQ39997958-FABC9B71-E89D-4E5B-B247-2F66BF799916Q41316169-038F352C-1097-413E-8FBA-550A3EAF94CAQ41887044-3BAA55F0-3D43-490B-A6AF-E76EDBD51948Q42183574-50759A86-CF17-4803-B749-F361252FDE58Q42211706-F4869863-ABBF-4872-854C-8AFADDE60888Q42393927-4761A329-91D5-414D-AF70-3765F0A2CB6DQ43016548-2864A99A-5FEC-4C45-BA88-8393186B1507Q43033703-69F010DD-A593-4F9A-A8C0-1D5D68976903Q46232464-09110BAA-35FC-4D21-921A-DA4DD69207A7Q46286002-2AFE3529-E2EB-487E-803C-3C21488B94BBQ46469402-4F56D208-43B6-4EEF-8BF3-82B6C43EBC26Q47192246-9E688B44-37D5-4C29-8D69-EADB69D41170Q47336519-076D79CE-8B97-4C6E-88DB-05F74A2CD43FQ48022764-91E0411F-6E72-4B57-A27C-55FB7201A23DQ48177497-95B21243-D0A3-4A33-98C6-8E8DB196E4FEQ48231696-059D5523-C466-4E37-A842-F6987ACB8635Q51744062-612DF807-433E-48AD-B367-55A463203190Q52643932-B7B784F5-BCF6-48BB-A667-0BB96304A38C
P2860
An extremely thermostable aldolase from Sulfolobus solfataricus with specificity for non-phosphorylated substrates.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
An extremely thermostable aldo ...... non-phosphorylated substrates.
@en
type
label
An extremely thermostable aldo ...... non-phosphorylated substrates.
@en
prefLabel
An extremely thermostable aldo ...... non-phosphorylated substrates.
@en
P2093
P2860
P356
P1433
P1476
An extremely thermostable aldo ...... non-phosphorylated substrates.
@en
P2093
P2860
P304
P356
10.1042/BJ3430563
P407
P478
P577
1999-11-01T00:00:00Z