✦ LIBER ✦

Evidence of a quinoprotein glucose dehydrogenase apoenzyme in several strains of Escherichia coli

✍ Scribed by R.W.J. Hommes; P.W. Postma; O.M. Neijssel; D.W. Tempest; P. Dokter; J.A. Duine

Book ID: 109312673
Publisher: John Wiley and Sons
Year: 1984
Tongue: English
Weight: 391 KB
Volume: 24
Category: Article
ISSN: 0378-1097
DOI: 10.1111/j.1574-6968.1984.tb01329.x

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Glucose metabolism by K+-limited Klebsie

Glucose metabolism by K+-limited Klebsiella aerogenes: Evidence for the involvement of a quinoprotein glucose dehydrogenase

✍ O.M. Neijssel; D.W. Tempest; P.W. Postma; J.A. Duine; J.Frank Jzn 📂 Article 📅 1983 🏛 John Wiley and Sons 🌐 English ⚖ 354 KB

Reconstitution of the quinoprotein gluco

Reconstitution of the quinoprotein glucose dehydrogenase from its apoenzyme on a gold electrode surface modified with a monolayer of pyrroloquinoline q

✍ Eugenii Katz; Daniela D. Schlereth; Hanns-Ludwig Schmidt; Arjen J.J. Olsthoorn 📂 Article 📅 1994 🏛 Elsevier 🌐 English ⚖ 828 KB

Role of quinoprotein glucose-dehydrogena

Role of quinoprotein glucose-dehydrogenase in gluconic acid production byAcinetobacter calcoaceticus

✍ J. A. M. Bont; P. Dokter; B. J. Schie; J. P. Dijken; J. Frank Jzn; J. Duine; J. 📂 Article 📅 1984 🏛 Springer Netherlands 🌐 English ⚖ 117 KB

Methanopterin is probably the first coenzyme involved in the reduction of CO 2 to CH 4 by Methanobacterium thermoautotrophicum. It is reduced and labelled with 14C02 in whole cells (Daniels and Zeikus, 1978; Keltjens et al., 1982) and it stimulates the formation of CH 4 in resolved cell-free extract

Cloning of a Serratia marcescens DNA fra

Cloning of a Serratia marcescens DNA fragment that induces quinoprotein glucose dehydrogenase-mediated gluconic acid production in Escherichia coli in the presence of stationary phase Serratia marcescens

✍ P.U. Krishnaraj; A.H. Goldstein 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 273 KB

Active-site changes in the pyruvate dehy

Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 Å resolution

✍ Chandrasekhar, Krishnamoorthy ;Arjunan, Palaniappa ;Sax, Martin ;Nemeria, Natali 📂 Article 📅 2006 🏛 International Union of Crystallography 🌐 English ⚖ 587 KB

The first enzymatic component, E1 (EC 1.2.4.1), of the pyruvate dehydrogenase multienzyme complex (PDHc) utilizes thiamine diphosphate (ThDP) and Mg(2+) as cofactors. The structure of a branched-chain-specific E1 apoenzyme from the heterotetrameric alpha(2)beta(2) E1 family was recently reported and

Proteomic study of antibiotic resistance

Proteomic study of antibiotic resistance in Escherichia coli strains

✍ P. Roncada; F. Deriu; A. Gaviraghi; P. A. Martino; L. Bonizzi 📂 Article 📅 2009 🏛 Springer Netherlands 🌐 English ⚖ 113 KB