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Macro-evolution of the G6PD molecule. This diagram reflects a synoptic analysis of 52 different G6PD sequences. Human G6PD is used as the reference
sequence and the even exons are underlined and numbered: the coding sequence starts in exon 2. In the lettering of human G6PD aa solvent accessibility
(SA) is reported with the following code: bold uppercase, buried aa (SA <10%), non-bolded uppercase, exposed aa (SA ≥10%). Immediately above the
human sequence we show the similarity consensus for the 52 sequences analyzed (Similarity), and above that the identity consensus sequence (Identity).
At each position the most frequent aa is shown, with a coding for its frequency (white uppercase in black field: 100%; black uppercase: 76–99%; white
lowercase in medium gray field: 51–75%); hyphens are entered in the two consensus lines for aa with <50% conservation. For aa similarity we have
Source: Glucose 6-Phosphate Dehydrogenase Deficiency, The Online Metabolic and Molecular Bases of Inherited Disease
adopted the criteria of the Dayhoff PAM 250 matrix, i.e.: (a) DEQHN, (b) FY, (c) KR, (d) SAT, and (e) LIVM. Conserved blocks described in the text are
Citation: Valle
Beaudet
AL, Vogelstein
KW,
Antonarakis
SE, Ballabio
K, Mitchell
Online
Metabolic
andβ-strands,
Molecular
boxed and identified
with D,
Roman
numerals.
Above B,
theKinzler
identity
consensus
sequence,
runs A,
ofGibson
underlined
a andG.
b The
indicate
α-helices
and
Bases
of
Inherited
Disease;
2014
Available
at:
http://mhmedical.com/
Accessed:
May
04,
2017
30
respectively, as found in the Leuconostoc mesenteroides molecule (Sec. structure). The N-terminal methionine is not present in the mature protein and
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Education.
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the N-terminal
alanine ©
is 2017
acetylated.
It is seen
that theAll
lysine
205
lies within a highly conserved stretch of amino acids. This residue is part of the G6Pbinding site. Also highly conserved is the NADP binding site at amino acids 38–44. Above the amino acid sequence the secondary structure is indicated by