FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1625798836> ?p ?o ?g. }

• W1625798836 endingPage "5927" @default.
• W1625798836 startingPage "5920" @default.
• W1625798836 abstract "Abstract A detailed comparison of the interactions of substrates with the mitochondrial and supernatant isozymes of glutamateaspartate transaminase (EC 2.6.1.1) has been made by direct spectrophotometric titrations of the natural reporter, bound pyridoxal phosphate, at the active site. Spectroscopic methods are presented for the analysis of the dissociation constants of the aspartate-oxalacetate and glutamate-α-ketoglutarate equilibria of mitochondrial glutamate-aspartate transaminase. Mathematical treatment of the spectrophotometric data is based on the assumption that the mechanism involves only binary complexes. The agreement and linearity of the graphical results of these methods rule out site-site interactions or the formation of ternary complexes, such as enzyme-amino acid-keto acid. The pyridoxal form of the mitochondrial isozyme has a higher affinity for aspartate (K1 = 0.47 mm) than for glutamate (K1 = 12.4 mm). It binds oxalacetate (K3 = 46 mm) and α-ketoglutarate (K3 = 620 mm) as inactive abortive complexes. In the supernatant enzyme these values are aspartate, K1 = 4 mm; glutamate, K1 = 14 mm; oxalacetate, K3 = 100 mm; and α-ketoglutarate, K3 = 50 mm. The pyridoxamine form of both isozymes binds oxalacetate (K2 = 14 µm, mitochondrial; K2 = 20 µm, supernatant) better than α-ketoglutarate (K2 = 0.7 mm, mitochondrial; K2 = 0.4 mm, supernatant), but it has a low affinity for glutamate and aspartate. The substrate analogue, erythro-β-hydroxyaspartate, forms a complex(es) with the mitochondrial aminotransferase which absorbs at 497 mµ. The affinity of the pyridoxal enzyme for this analogue (K = 0.2 mm) is comparable to that of aspartate and is lower than in the supernatant enzyme (K = 0.4 mm). The pyridoxamine form of each isozyme has a higher affinity for erythro-β-hydroxyaspartate than for either glutamate or aspartate. Radioactive exchange studies indicate that transamination can occur between the substrate amino acid and its analogous keto acid. Dissociation constants obtained by this method agree with those of steady state equilibrium spectrophotometric data. A comparison of the intermediates of the mitochondrial and supernatant glutamate-aspartate transaminase indicates that the mitochondrial isozyme has a high affinity for 4-carbon substrates, whereas the supernatant enzyme has no distinctive preference for either 4- or 5-carbon substrates." @default.
• W1625798836 created "2016-06-24" @default.
• W1625798836 creator A5030868094 @default.
• W1625798836 creator A5088647701 @default.
• W1625798836 date "1969-11-01" @default.
• W1625798836 modified "2023-10-18" @default.
• W1625798836 title "Distinctions in the Equilibrium Kinetic Constants of the Mitochondrial and Supernatant Isozymes of Aspartate Transaminase" @default.
• W1625798836 cites W152081146 @default.
• W1625798836 cites W1544099313 @default.
• W1625798836 cites W1548912836 @default.
• W1625798836 cites W1552971764 @default.
• W1625798836 cites W1560037751 @default.
• W1625798836 cites W1560284252 @default.
• W1625798836 cites W1856142962 @default.
• W1625798836 cites W1969827595 @default.
• W1625798836 cites W1975143963 @default.
• W1625798836 cites W1985674503 @default.
• W1625798836 cites W1986123823 @default.
• W1625798836 cites W2030547353 @default.
• W1625798836 cites W2035459627 @default.
• W1625798836 cites W2049049929 @default.
• W1625798836 cites W2066351462 @default.
• W1625798836 cites W2070672758 @default.
• W1625798836 cites W2341009984 @default.
• W1625798836 cites W41862321 @default.
• W1625798836 cites W75328843 @default.
• W1625798836 cites W75600392 @default.
• W1625798836 doi "https://doi.org/10.1016/s0021-9258(18)63560-4" @default.
• W1625798836 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/5350945" @default.
• W1625798836 hasPublicationYear "1969" @default.
• W1625798836 type Work @default.
• W1625798836 sameAs 1625798836 @default.
• W1625798836 citedByCount "60" @default.
• W1625798836 countsByYear W16257988362014 @default.
• W1625798836 countsByYear W16257988362018 @default.
• W1625798836 crossrefType "journal-article" @default.
• W1625798836 hasAuthorship W1625798836A5030868094 @default.
• W1625798836 hasAuthorship W1625798836A5088647701 @default.
• W1625798836 hasBestOaLocation W16257988361 @default.
• W1625798836 hasConcept C10710636 @default.
• W1625798836 hasConcept C119795356 @default.
• W1625798836 hasConcept C121332964 @default.
• W1625798836 hasConcept C135889238 @default.
• W1625798836 hasConcept C147789679 @default.
• W1625798836 hasConcept C181199279 @default.
• W1625798836 hasConcept C185592680 @default.
• W1625798836 hasConcept C2776877979 @default.
• W1625798836 hasConcept C55493867 @default.
• W1625798836 hasConcept C62520636 @default.
• W1625798836 hasConcept C97355855 @default.
• W1625798836 hasConceptScore W1625798836C10710636 @default.
• W1625798836 hasConceptScore W1625798836C119795356 @default.
• W1625798836 hasConceptScore W1625798836C121332964 @default.
• W1625798836 hasConceptScore W1625798836C135889238 @default.
• W1625798836 hasConceptScore W1625798836C147789679 @default.
• W1625798836 hasConceptScore W1625798836C181199279 @default.
• W1625798836 hasConceptScore W1625798836C185592680 @default.
• W1625798836 hasConceptScore W1625798836C2776877979 @default.
• W1625798836 hasConceptScore W1625798836C55493867 @default.
• W1625798836 hasConceptScore W1625798836C62520636 @default.
• W1625798836 hasConceptScore W1625798836C97355855 @default.
• W1625798836 hasIssue "21" @default.
• W1625798836 hasLocation W16257988361 @default.
• W1625798836 hasOpenAccess W1625798836 @default.
• W1625798836 hasPrimaryLocation W16257988361 @default.
• W1625798836 hasRelatedWork W1550996414 @default.
• W1625798836 hasRelatedWork W1761774275 @default.
• W1625798836 hasRelatedWork W1897792778 @default.
• W1625798836 hasRelatedWork W2010682410 @default.
• W1625798836 hasRelatedWork W2037443437 @default.
• W1625798836 hasRelatedWork W2050182051 @default.
• W1625798836 hasRelatedWork W2060038873 @default.
• W1625798836 hasRelatedWork W2142386704 @default.
• W1625798836 hasRelatedWork W2318424018 @default.
• W1625798836 hasRelatedWork W903917906 @default.
• W1625798836 hasVolume "244" @default.
• W1625798836 isParatext "false" @default.
• W1625798836 isRetracted "false" @default.
• W1625798836 magId "1625798836" @default.
• W1625798836 workType "article" @default.