Dimeric Crystal Structure of Rabbit l-Gulonate 3-Dehydrogenase/λ-Crystallin: Insights into the Catalytic Mechanism

Asada, Yujiro; Kuroishi, Chizu; Ukita, Yoko; Sumii, Rie; Endo, Shunsuke; Matsunaga, Toshiyuki; Hara, Akira; Kunishima, N.

doi:10.1016/j.jmb.2010.06.069

Cited by 6 publications

(7 citation statements)

References 41 publications

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“…From an evolutionary point of view, these proteins served an initial function and were exapted to serve additional roles. A well-known example are the crystallin proteins in the eye that evolved from various dehydrogenases to serve as structural proteins that increase the transparency and refractive index of light (Asada et al, 2010). These gene products assumed their alternate functions based on a cell that evolved a mechanism to accommodate this purpose.…”

Section: Introductionmentioning

confidence: 99%

Regulation of MIF Enzymatic Activity by an Allosteric Site at the Central Solvent Channel

Pantouris

Khurana

et al. 2020

Cell Chemical Biology

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Section: Introductionmentioning

confidence: 99%

Regulation of MIF Enzymatic Activity by an Allosteric Site at the Central Solvent Channel

Pantouris

Khurana

et al. 2020

Cell Chemical Biology

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“…FHMPCDH showed significant similarity to those of the HAD family. In addition, FHMPCDH also showed identity to those of DKR, a member of dicarbonyl reductases [30], and RGHD, a member of the GDH/cCRY family [31] as described below. The three sequences highly homologous to that of FHMPCDH are aligned in Supplemental Fig.…”

Section: Amino Acid Sequence Comparison With Other Enzymesmentioning

confidence: 88%

“…A DALI search [32] using the monomer structure of FHMPCDH shows high similarity to RGHD [31], followed by diketoreductase [19] and (S)-3-hydroxybutyryl-CoA dehydrogenase (HBDH) from Clostridium butyricum [33] (Supplemental Table S1). The major difference was on the C-terminal domain: FHMPCDH contains an extra helix in the C-terminal domain (a11) (Supplemental Fig.…”

Section: -Pyridoxic Acid 5-formyl-3-hydroxy-2-methyl Pyridine-4-carbmentioning

confidence: 99%

Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD+-dependent dismutase from Mesorhizobium loti

Mugo

Kobayashi

Mikami

et al. 2015

Biochemical and Biophysical Research Communications

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“…The present study involves the rabbit lens, which contains high levels of the UVA-absorbing pyridine nucleotide NADH, both free and bound to λ-crystallin (Bando et al, 2006; Giblin and Reddy, 1980; Zigler and Rao, 1991). Rabbit lens λ-crystallin is identical to the liver enzyme L-gulonate 3-dehydrogenase whose crystal structure in complex with NADH has been determined at 1.85 Å resolution (Asada et al, 2010; Ishikura et al, 2005). …”

Section: Introductionmentioning

confidence: 99%

A Class I UV-blocking (senofilcon A) soft contact lens prevents UVA-induced yellow fluorescence and NADH loss in the rabbit lens nucleus in vivo

Giblin¹,

Lin²,

Simpanya³

et al. 2012

Experimental Eye Research

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It is known that fluorescence, much of it caused by UVA light excitation, increases in the aging human lens, resulting in loss of sharp vision. This study used an in vivo animal model to investigate UVA-excited fluorescence in the rabbit lens, which contains a high level of the UVA chromophore NADH, existing both free and bound to λ-crystallin. Also, the ability of a Class I (senofilcon A) soft contact lens to protect against UVA-induced effects on the rabbit lens was tested. Rabbit eyes were irradiated with UVA light in vivo (100 mW/cm2 on the cornea) for 1 hour using monochromatic 365 nm light. Irradiation was conducted in the presence of either a senofilcon A contact lens, a minimally UV-absorbing lotrafilcon A contact lens, or no contact lens at all. Eyes irradiated without a contact lens showed blue 365 nm-excited fluorescence initially, but this changed to intense yellow fluorescence after 1 hour. Isolated, previously irradiated lenses exhibited yellow fluorescence originating from the lens nucleus when viewed under 365 nm light, but showed normal blue fluorescence arising from the cortex. Previously irradiated lenses also exhibited a faint yellow color when observed under visible light. The senofilcon A contact lens protected completely against the UVA-induced effects on fluorescence and lens yellowing, whereas the lotrafilcon A lens showed no protection. The UVA-exposure also produced a 53% loss of total NADH (free plus bound) in the lens nucleus, with only a 13% drop in the anterior cortex. NADH loss in the nucleus was completely prevented with use of a senofilcon A contact lens, but no significant protection was observed with a lotrafilcon A lens. Overall, the senofilcon A lens provided an average of 67% protection against UVA-induced loss of four pyridine nucleotides in four different regions of the lens. HPLC analysis with fluorescence detection indicated a nearly six-fold increase in 365 nm-excited yellow fluorescence arising from lens nuclear λ-crystallin after the in vivo UVA exposure. It is concluded that UVA-induced loss of free NADH (which fluoresces blue) may have allowed the natural yellow fluorescence of λ-crystallin and other proteins in the lens nucleus to become visible. Increased fluorescence exhibited by UVA-exposed λ-crystallin may have been the result of a UVA-induced change in the conformation of the protein occurring during the initial UVA-exposure in vivo. The results demonstrate the greater susceptibility of the lens nucleus to UVA-induced stress, and may relate to the formation of human nuclear cataract. The senofilcon A contact lens was shown to be beneficial in protecting the rabbit lens against effects of UVA light, including changes in fluorescence, increased yellowing and loss of pyridine nucleotides.

show abstract

Dimeric Crystal Structure of Rabbit l-Gulonate 3-Dehydrogenase/λ-Crystallin: Insights into the Catalytic Mechanism

Cited by 6 publications

References 41 publications

Regulation of MIF Enzymatic Activity by an Allosteric Site at the Central Solvent Channel

Regulation of MIF Enzymatic Activity by an Allosteric Site at the Central Solvent Channel

Crystal structure of 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase, an NAD+-dependent dismutase from Mesorhizobium loti

A Class I UV-blocking (senofilcon A) soft contact lens prevents UVA-induced yellow fluorescence and NADH loss in the rabbit lens nucleus in vivo

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