Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures.

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures. Abstract Text:

T Tanaka,S Yamamoto,M Taniguchi,H Hayashi,S Kuramitsu,H Kagamiyama,S Oi,

Aspartate aminotransferase (AspAT) [EC 2.6.1.1] of thermophilic methanogen was further characterized with the enzyme from Methanobacterium thermoautotrophicum strain FTF-INRA as well as M. thermoformicicum strain SF-4. AspAT of strain FTF-INRA was similar in the amino donor specificity to the enzyme of M. thermoformicicum strain SF-4, in that it was active on L-cysteine and L-cysteine sulfinate in addition to L-glutamate and L-aspartate. The enzymes gave similar absorption spectra having maxima at around 326 and 415 nm with no pH-dependent shift but were found to contain 1 mol of tightly bound pyridoxal 5'-phosphate (PLP) per subunit. Reconstitution of each apoenzyme with added PLP resulted in partial recovery of the original enzymatic activity, suggesting a significant conformational change of the active site region upon removal of the cofactor. Polyacrylamide gel electrophoresis (PAGE) and gel filtration analyses revealed a tetrameric structure (180 kDa) of identical subunits with a molecular mass of 43 kDa for each of these enzymes. Electric current was found to affect the interaction or affinity of each subunit, promoting dissociation of the native enzyme into the monomeric form. Alkaline treatment was effective only for dissociation of the enzyme from strain SF-4. They were distinguishable by the more rapid reassociation of the monomer to the native aggregated form in the enzyme of strain FTF-INRA.

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures. Publishing Authors By Initials

T Tanaka,S Yamamoto,M Taniguchi,H Hayashi,S Kuramitsu,H Kagamiyama,S Oi,

For similar investigative techniques: chemistry, analytical: photometry: spectrophotometry research abstracts see: investigative techniques: chemistry, analytical: photometry: spectrophotometry research

PUBMED ID PMID:

MEDLINE DATE:

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 112

Page Numbers: 811-5

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1992

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures. Keywords Mesh Terms:

KEYWORDS: Spectrophotometry

MESH TERMS: enzymology

Chemical & Substance for Abstract: Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures. Information

Substance Name: Aspartate Aminotransferases

Registry Number: EC 2.6.1.1

Grant and Affiliation Information for Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures.

AFFILIATION: Department of Biology, Faculty of Science, Osaka City University.

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures Related Publications

• Aspartate aminotransferase from a thermophilic formate-utilizing methanogen, Methanobacterium thermoformicicum strain SF-4: relation to serine and phosphoserine aminotransferases, but not to the aspartate aminotransferase family.
• Further studies on aspartate aminotransferase of thermophilic methanogens by analysis of general properties, bound cofactors, and subunit structures.
• Greater incidence of emergence agitation in children after sevoflurane anesthesia as compared with halothane: a meta-analysis of randomized controlled trials.
• Hepatic embolization from the common hepatic artery using balloon occlusion technique.
• Inhibition of bovine liver rhodanese by alpha-ketoglutarate.
• Inhibition of rat liver rhodanese by di-, tricarboxylic, and alpha-keto acids.
• Management of exaggerated gag reflex using intravenous sedation in prosthodontic treatment.
• Molecular and biochemical markers for monitoring dynamic shifts of cellulolytic protozoa in Reticulitermes flavipes.
• Potassium-stimulating mechanism of geranylgeranyl diphosphate synthase of Methanobacterium thermoformicicum SF-4.
• Prevalence of Ovarian Cancer among Women with a CA125 Level of 35 U/ml or Less.
• Purification and some properties of beta-transglycosylase of Trichoderma longibrachiatum.
• Sonographic evaluation of hydatidiform mole and its look-alikes.
• The infrared characteristic absorption bands of monosubstituted naphthalenes in the region of 1650-2000 cm-1.
• [Advisability of surgery in stomach diseases.]